"Hairpin Oligonucleotides" Cross-reference to related applications The present application claims priority from Australian Provisional Patent Application No. 2022902346 filed on 17 August 2022, the contents of which is incorporated herein by reference in its entirety. Technical field The present disclosure relates to the field of oligonucleotides. More particularly, the present disclosure relates to hairpin oligonucleotides for the specific binding and inhibition of target proteins, such as transcription factors. Additionally, this disclosure relates to methods of using such oligonucleotides in preventing or treating diseases, disorders or conditions associated with such target proteins. Background Nucleic acid binding proteins, such as transcription factors, can play a role at various points in cell signalling pathways, so as to modulate many normal cellular processes, such as cell growth and proliferation, metabolism, apoptosis, immune responses, and differentiation. Given these cellular effects, their activity is often found to be deregulated in disease, such as cancer. As such, targeting this class of proteins is a major focus of interest, but the structural disorder and lack of binding pockets have made the rational design of small molecule inhibitors for transcription factors challenging. Accordingly, there remains a need for new inhibitors of nucleic acid binding proteins, and particularly those that can specifically target transcription factor activity. Summary The present disclosure is based on the surprising finding that a hairpin oligonucleotide that includes a consensus cMyc binding site in its stem region can specifically bind to this transcription factor with high affinity and inhibit its proliferative effects in cancer cells. Such an inhibition strategy may be applied to other transcription factors that bind to specific nucleic acid sequences, structures or motifs with high affinity. In a first aspect, the present disclosure provides a hairpin oligonucleotide for inhibiting a target protein, the hairpin oligonucleotide comprising a loop region and a stem region, wherein the stem region comprises a binding site for the target protein. Suitably, the target protein is a transcription factor, such as an E-box transcription factor. In some examples, the transcription factor is selected from the group consisting of Myc, Myc/Max, Fos/Jun, HIF1α/β, MITF, MyoD, HES family, Hey family, ID1/2/3, E2 family, Twist, AHR, AHRR, ARNT, ARNT2, ARNTL, ARNTL2, ASCL1, ASCL2, ASCL3, ASCL4, ATF1, ATF2, ATF4, ATF5, ATF6, ATF7, ATOH1, ATOH7, ATOH8, BACH1, BACH2, BATF, BATF2, BHLHB2, BHLHB3, BHLHB4, BHLHB5, BHLHB8, CLOCK, CREB1, CREB3, CREB3L1, CREB3L2, CREB3L3, CREB3L4, CREB5, CREBL1, CREM, E4BP4, EPAS1, FERD3L, FIGLA, FOSL1, FOSL2, HAND1, HAND2, HES1, HES2, HES3, HES4, HES5, HES6, HES7, HEY1, HEY2, HIF1A, ID1, ID2, ID3, ID4, JUN, JUNB, JUND, KIAA2018, LYL1, MASH1, MATH2, MAX, MESP1, MESP2, MIST1, MITF, MLX, MLXIP, MLXIPL, MNT, MSC, MSGN1, MXD1, MXD3, MXD4, MXI1, MYC, MYCL1, MYCL2, MYCN, MYF5, MYF6, MYOD1, MYOG, NCOA1, NCOA3, NEUROD1, NEUROD2, NEUROD4, NEUROD6, NEUROG1, NEUROG2, NEUROG3, NFE2, NFE2L2, NFE2L3, NHLH1, NHLH2, NPAS1, NPAS2, NPAS3, OAF1, OLIG1, OLIG2, OLIG3, OPAQUE2, PTF1A, SCL, SCXB, SIM1, SIM2, SNFT, SOHLH1, SOHLH2, SREBF1, SREBF2, TAL1, TAL2, TCF12, TCF15, TCF21, TCF3, TCF4, TCFL5, TFAP4, TFE3, TFEB, TFEC, TWIST1, TWIST2, USF1, USF2 and any combination thereof. In one example, the transcription factor is Myc or Myc/Max. Suitably, the binding site comprises, consists of or consists essentially of the nucleic acid sequence of 5'-CAC[GA]TG-3', 5'-CAC[GA]UG-3' or a fragment, variant or derivative thereof. In certain examples, the binding site of the hairpin oligonucleotide comprises, consists of or consists essentially of the nucleic acid sequence of 5'-GAGCACGUGGUU-3' (SEQ ID NO: 3) or a fragment, variant or derivative thereof and wherein one or more of the U nucleotides thereof may be a T. Suitably, the hairpin oligonucleotide comprises, consists of or consists essentially of the nucleotide sequence of SEQ ID NO: 1 or a fragment, variant or derivative thereof. In some examples, the stem region comprises a sense strand and an antisense strand, each strand having 5 to 50 nucleotides. In other examples, the hairpin oligonucleotide comprises one or a plurality of phosphorothioate internucleotide linkages. Suitably, the hairpin oligonucleotide comprises one or a plurality of modified nucleotides. In certain examples, the one or plurality of modified nucleotides comprise a modification selected from the group consisting of LNA, HNA, CeNA, 2’-methoxyethyl, 2’-O-alkyl, 2’-O-allyl, 2’- C- allyl, 2’-fluoro, 2’-deoxy, and combinations thereof. In various examples, one or more of the modified nucleotides are modified with 2’-OCH ₃ . In a second aspect, the present disclosure provides a pharmaceutical composition comprising the hairpin oligonucleotide of the first aspect and a pharmaceutically-acceptable carrier, diluent or excipient. In a third aspect, the present disclosure relates to a method of inhibiting a target protein of a cell, said method including the step of contacting the cell with the hairpin oligonucleotide of the first aspect or the pharmaceutical composition of the second aspect. In a fourth aspect, the present disclosure provides for the use of the hairpin oligonucleotide of the first aspect or the pharmaceutical composition of the second aspect in the manufacture of a medicament for inhibiting a target protein of a cell. In a fifth aspect, the present disclosure resides in a method of preventing, ameliorating or treating a disease, disorder or condition associated with a target protein in a subject, said method including the step of administering to the subject a therapeutically effective amount of the hairpin oligonucleotide of the first aspect or the pharmaceutical composition of the second aspect to thereby prevent, ameliorate or treat the disease, disorder or condition. In a sixth aspect, the present disclosure relates to the use of the hairpin oligonucleotide of the first aspect or the pharmaceutical composition of the second aspect in the manufacture of a medicament for preventing, ameliorating or treating a disease, disorder or condition associated with a target protein in a subject. Referring to the fifth and sixth aspects, the disease, disorder or condition suitably is or comprises a cancer. In some examples, the cancer is selected from the group consisting of breast cancer, lung cancer, ovarian cancer, cervical cancer, uterine cancer, prostate cancer, cancer of the brain and nervous system, head and neck cancer, colon cancer, colorectal cancer, gastric cancer, liver cancer, kidney cancer, melanoma, skin carcinoma, lymphoid cancer, myelomonocytic cancer, pancreatic cancer, pituitary cancer, bone cancer and soft tissue cancer. In one example, the cancer is or comprises breast cancer. In a seventh aspect, the present disclosure provides a method for selecting a hairpin oligonucleotide for inhibiting a target protein, said method including the steps of: (a) producing one or more candidate hairpin oligonucleotides comprising a loop region and a stem region, wherein the stem region comprises a binding site for the target protein; (b) testing the ability of the one or more candidate hairpin oligonucleotides to inhibit the target protein, and (c) selecting a hairpin oligonucleotide which binds and/or inhibits the target protein. In an eighth aspect, the present disclosure relates to a hairpin oligonucleotide designed, selected or identified by the method of the seventh aspect. Brief description of the drawings The following figures form part of the present specification and are included to further demonstrate certain aspects of the present disclosure. The disclosure may be better understood by reference to one or more of these figures in combination with the detailed description of specific embodiments presented herein. It will be appreciated by persons skilled in the art that numerous variations and/or modifications may be made to the above-described embodiments, without departing from the broad general scope of the present disclosure. The present embodiments are, therefore, to be considered in all respects as illustrative and not restrictive. Figure 1: DRpinMYC forms a stable A-form hairpin. (A) Solution structure of the top cluster of DRpinMYC from a 1 μs atomistic molecular dynamics simulation. Solvent not shown. Bases are labelled according to the sequence's 5' to 3' position. (B) Diagrammatic secondary structure representation of DRpinMYC from MC-Fold composed of twelve Watson-Crick base pairs with a four-base poly-Adenosine loop and blunt ends. (C) MC-Fold generated dot-bracket notation of secondary structure of DRpinMYC. Scoring indicates a highly stable structure. Figure 2: Binding of DRpin to cMyc:Max dimer. (Left panel) Graph of densitometry of cMyc binding to DRpin-Myc; (Right panel) Graph of densitometry of the Myc:Max dimer binding to DRpin-Myc. NegC is an oligonucleotide of the same chemistry, but lacking the Myc consensus sequence (random sequence). Y axis is relative DRpin-Myc bound by Myc or Myc:Max. X axis is nM of Myc or Myc:Max. Figure 3: A diagram depicting the proposed binding of DRpinMyc with cMyc:Max. Modelling is consistent with the EMSA assays. It suggests the self folding RNA DRpin-Myc molecule can be bound by the cMyc:Max heterodimer. Figure 4: DRpinMyc was used to treat a number of breast cancer cell lines. The drug was either used after resuspension with no additional input other than the buffer or the dissolved drug was heated to 90 ^o C and allowed to cool over 1 hours. This was to determine if DRpinMyc was indeed self folding with no intervention or if it would need an annealing stage. The annealed experiments are labelled with an A (e.g., D2-A). Figure 5: Incucyte analysis of cell growth rate when treated with redissolved DRpinMyc or when treated with re-annealed DRpinMyc. As can be observed DRpinMyc inhibits cell expansion and growth at varying concentrations depending on the cell line. This is consistent with a siMyc treated cells, which arrest in the cell cycle. Figure 6: Cell cycle analysis was performed by flow cytometry using the PI stain. It indicated that like siRNA deletion of cMyc that the cell arrested at different stages of the cell cycle. A represents a 48 hour time point and B a 120 hour time points. The later time points showed that cells were beginning to die. Figure 7: Venn diagram representation of DE genes (fold change beyond +1 and Padj < 0.05) across all contrasts. Figure 8: Heatmap of upregulated transcription factors: Shown are the significantly upregulated transcription factors. The colour scale bar shows z-score values after z-score row normalization. Heatmap was generated using pheatmap package from R. Figure 9: Heatmap of down regulated transcription factors: Shown are the significantly down regulated transcription factors. The colour scale bar shows z-score values after z-score row normalization. Heatmap was generated using pheatmap package from R. Figure 10: DRpin-Myc significantly inhibited TNBC PDX tumour growth. Figure 11: DRpin-Myc significantly inhibited tumour growth in an MDA-MB-231-based xenograft model. Figure 12: MM/PBSA thermodynamic cycle. MM/PBSA thermodynamic cycle of protein in green and ligand in yellow. Adapted from the Amber Tools 16 manual. Figure 13: Top clusters of oligonucleotides and the MYC: MAX complex. The top representative cluster of each system, derived from 2 μs simulations performed in triplicate. Each system represents a total 6 μs. Myc and Max bHLH/LZ domains are indicated by purple and pink ribbon structures, respectively. A green and yellow ladder structure indicates the DNA duplex. A green ladder structure alone indicates DRpinMYC stereoisomers. The red ladder structure indicates the E-box duplex in each system. Representations of top clusters proportion, cluster RMSD and buried SASA between the complex and DRpinMYC are provided below. Figure 14: MM/GBSA energy decomposition of MYC: MAX systems. Decomposition heatmaps from oligonucleotide, MYC: MAX trajectories. Energies are derived from MM/GBSA calculations and represent 6 μs total per system. MYC, MAX and oligonucleotide 5′, 3′ E-box and loops are marked accordingly. Protein end residues that contributed >-0.2 kcal/mol to binding energies were removed. All energies are presented in kcal/mol and indicated per the colour bar. Key to the Sequence Listing SEQ ID NO: 1 Nucleotide sequence of DRpinMyc in Figure 1 SEQ ID NO: 2 Amino acid sequence of cMyc protein SEQ ID NO: 3 Nucleotide sequence of binding site in DRpinMyc SEQ ID NO: 4 Nucleotide sequence of consensus E-box binding site SEQ ID NO: 5 Nucleotide sequence of exemplary E-box binding site #1 SEQ ID NO: 6 Nucleotide sequence of exemplary E-box binding site #2 SEQ ID NO: 7 Nucleotide sequence of exemplary E-box binding site #3 SEQ ID NO: 8 Nucleotide sequence of non-canonical E-box binding site #1 SEQ ID NO: 9 Nucleotide sequence of non-canonical E-box binding site #2 SEQ ID NO: 10 Nucleotide sequence of non-canonical E-box binding site #3 SEQ ID NO: 11 Nucleotide sequence of exemplary E-box binding site #4 SEQ ID NO: 12 Nucleotide sequence of exemplary E-box binding site #5 SEQ ID NO: 13 Nucleotide sequence of exemplary E-box binding site #6 SEQ ID NO: 14 Nucleotide sequence of consensus E-box binding site #2 SEQ ID NO: 15 Nucleotide sequence of non-canonical E-box binding site #4 SEQ ID NO: 16 Nucleotide sequence of non-canonical E-box binding site #5 SEQ ID NO: 17 Nucleotide sequence of non-canonical E-box binding site #6 SEQ ID NO: 18 Nucleotide sequence of non-canonical E-box binding site #7 SEQ ID NO: 19 Nucleotide sequence of non-canonical E-box binding site #8 SEQ ID NO: 20 Nucleotide sequence of non-canonical E-box binding site #9 SEQ ID NO: 21 Nucleotide sequence of non-canonical E-box binding site #10 SEQ ID NO: 22 Nucleotide sequence of non-canonical E-box binding site #11 SEQ ID NO: 23 Nucleotide sequence of non-canonical E-box binding site #12 SEQ ID NO: 24 Nucleotide sequence of binding site in DRpinMyc variant #1 SEQ ID NO: 25 Nucleotide sequence of binding site in DRpinMyc variant #2 SEQ ID NO: 26 Nucleotide sequence of binding site in DRpinMyc variant #3 SEQ ID NO: 27 Nucleotide sequence of binding site in DRpinMyc variant #4 SEQ ID NO: 28 Nucleotide sequence of binding site in DRpinMyc variant #5 SEQ ID NO: 29 Nucleotide sequence of binding site in DRpinMyc variant #6 SEQ ID NO: 30 Nucleotide sequence of binding site in DRpinMyc variant #7 SEQ ID NO: 31 Nucleotide sequence of binding site in DRpinMyc variant #8 SEQ ID NO: 32 Nucleotide sequence of binding site in DRpinMyc variant #9 Detailed description General Techniques and Definitions Unless specifically defined otherwise, all technical and scientific terms used herein shall be taken to have the same meaning as commonly understood by one of ordinary skill in the art (e.g., in genomics, immunology, molecular biology, immunohistochemistry, biochemistry, oncology, and pharmacology). The present disclosure is performed without undue experimentation using, unless otherwise indicated, conventional techniques of molecular biology, microbiology, recombinant DNA technology and immunology. Such procedures are described, for example in Sambrook, Fritsch & Maniatis, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratories, New York, Fourth Edition (2012), whole of Vols I, II, and III; DNA Cloning: A Practical Approach, Vols. I and II (D. N. Glover, Second Edition., 1995), IRL Press, Oxford, whole of text; Oligonucleotide Synthesis: A Practical Approach (M. J. Gait, ed, 1984) IRL Press, Oxford, whole of text, and particularly the papers therein by Gait, ppl-22; Atkinson et al, pp35-81; Sproat et al, pp 83-115; and Wu et al, pp 135-151; 4. Nucleic Acid Hybridization: A Practical Approach (B. D. Hames & S. J. Higgins, eds., 1985) IRL Press, Oxford, whole of text; Immobilized Cells and Enzymes: A Practical Approach (1986) IRL Press, Oxford, whole of text; Perbal, B., A Practical Guide to Molecular Cloning (1984) and Methods In Enzymology (S. Colowick and N. Kaplan, eds., Academic Press, Inc.), whole of series. Those skilled in the art will appreciate that the present disclosure is susceptible to variations and modifications other than those specifically described. It is to be understood that the disclosure includes all such variations and modifications. The disclosure also includes all of the steps, features, compositions and compounds referred to or indicated in this specification, individually or collectively, and any and all combinations of any two or more of said steps or features. The present disclosure is not to be limited in scope by the specific embodiments described herein, which are intended for the purpose of exemplification only. Functionally equivalent products, compositions and methods are clearly within the scope of the disclosure, as described herein. Each feature of any particular aspect or embodiment or embodiment of the present disclosure may be applied mutatis mutandis to any other aspect or embodiment or embodiment of the present disclosure. Throughout this specification, unless specifically stated otherwise or the context requires otherwise, reference to a single step, composition of matter, group of steps or group of compositions of matter shall be taken to encompass one and a plurality (i.e., one or more) of those steps, compositions of matter, groups of steps or group of compositions of matter. As used herein, the singular forms of “a”, “and” and “the” include plural forms of these words, unless the context clearly dictates otherwise. For example, a reference to “a bacterium” includes a plurality of such bacteria, and a reference to “an allergen” is a reference to one or more allergens. The term “and/or”, e.g., “X and/or Y” shall be understood to mean either “X and Y” or “X or Y” and shall be taken to provide explicit support for both meanings or for either meaning. As used herein, the term about, unless stated to the contrary, refers to +/- 10%, more preferably +/-5%, even more preferably +/-1%, of the designated value. Throughout this specification, the word “comprise’ or variations such as “comprises” or “comprising” will be understood to imply the inclusion of a stated element, integer or step, or group of elements, integers or steps, but not the exclusion of any other element, integer or step, or group of elements, integers or steps. By “consisting essentially of”, in the context of: (a) an amino acid sequence, is meant the recited amino acid sequence together with an additional one, two or three amino acids at the N- and/or C-terminus thereof; or (b) a nucleic acid sequence, is meant the recited nucleic acid sequence together with an additional one, two or three nucleic acids at the 5’ and/or 3’ thereof. All computer programs, algorithms, patent and scientific literature referred to herein is incorporated herein by reference. For the present disclosure, the database accession number or unique identifier provided herein for a gene or protein, as well as the gene and/or protein sequence or sequences associated therewith, are incorporated by reference herein. Hairpin oligonucleotides The inventors has surprisingly shown that hairpin oligonucleotides that incorporate a consensus binding site for a target nucleic acid binding protein can be utilised to bind and functionally deplete the target protein and thereby inhibit a biological activity thereof, such as cell growth or proliferation. Accordingly, in one form, there is provided herein a hairpin oligonucleotide for inhibiting a target protein, the hairpin oligonucleotide comprising a loop region and a stem region, wherein the stem region comprises a binding or recognition site for the target protein. In the context of this disclosure, the term “oligonucleotide” refers to an oligomer or polymer of ribonucleic acid (RNA) or deoxyribonucleic acid (DNA), wherein the polymer or oligomer of nucleotide monomers contains any combination of nucleobases (referred to in the art and herein as simply as “base”), modified nucleobases, sugars, modified sugars, phosphate bridges, or modified phosphorus atom bridges (also referred to herein as “internucleotide linkage”). Oligonucleotides can be single-stranded or double-stranded or a combination thereof. A single- stranded oligonucleotide can have double-stranded regions and a double-stranded oligonucleotide can have single-stranded regions (such as a microRNA or shRNA). The terms “hairpin oligo” or “hairpin oligonucleotide” are used interchangeably herein and refer to a nucleic acid molecule, which has a segment (also known as a “hairpin loop” or “loop region”) that is not hybridized with or complementary to a segment of the same hairpin oligonucleotide, and a double-stranded linear region (also known as a “stem” or “duplex” region) having segments that are complementary to each other in the same molecule. Accordingly, the hairpin oligonucleotide suitably comprises a single-stranded loop region that is positioned between a first self-complementary region (e.g., a sense strand) and a second self- complementary region (e.g., an antisense strand) that define, at least in part, the stem region. The hairpin structure of the oligonucleotides described herein is advantageous, as a double stranded oligo of the same chemistry, once entering cells, would have the propensity to equilibrate between corresponding double stranded and single stranded nucleotide structures. Once no longer hybridized in a double stranded manner, a single stranded nucleic acid would further likely not re-anneal to its complementary single stranded nucleic acid due to the dilution factor within a cell. A hairpin oligonucleotide that melts, denatures or dissociates will still maintain a localised high concentration of the respective complementary single stranded stem sequences, which would favour reannealing and formation of the double stranded stem region. In addition, double stranded oligonucleotides that melt, denature or dissociate will have the potential to anneal to homologous RNA and DNA molecules giving the potential for off target activity and/or the mopping up of the single stranded portions of the oligonucleotide preventing them from reannealing to form a double stranded structure. Conversely, the hairpin oligonucleotide provided herein would be less likely to bind/hybridise and/or interact with other off-target nucleic acids, because: (a) the corresponding sequence with the greatest homology is within the same molecule; and (b) the size of the hairpin oligonucleotide reduces its propensity to bind to short complementary nucleic acids. Oligonucleotides generally refer to relatively short sequences of nucleotides, typically with twenty or fewer bases (or nucleotide units), but can also be significantly longer, such as up to about 160 to about 200 nucleotides. By way of example, the hairpin oligonucleotide provided herein is at least about 3, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 45, 50, 60, 70, 80, 90, 100 nucleotides, or any range therein, in length as a single stranded molecule. More particularly, the hairpin oligonucleotide is suitably about 3 to about 75 nucleotides (e.g., about 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 65, 70, or 75 nucleotides, or any range therein) in length as a single stranded molecule. In various examples, the hairpin oligonucleotide is about 15 to about 56, more particularly about 20 to about 40, even more particularly about 25 to about 35, nucleotides in length as a single stranded molecule. In some examples, the hairpin oligonucleotide is about 28 nucleotides in length as a single stranded molecule. Suitably, the stem region is of sufficient length to incorporate a binding site for the target protein. To this end, the stem region (i.e., the double stranded linear or duplex region) provided herein is at least about 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 45, 50 nucleotide pairs, or any range therein, in length. More particularly, the stem region can be about 6 to about 20 nucleotide pairs in length. Even more particularly, the stem region can be about 8 to about 15 nucleotide pairs in length. Yet even more particularly, the stem region can be about 10 to about 14 nucleotide pairs in length. In certain examples, the stem region is about 12 nucleotide pairs in length. According to various examples, the stem region provided herein is stable (i.e., the self- complementary regions are capable of remaining hybridized together) at approximately 37°C, and unhybridize (i.e., denature) at temperatures greater than 50°C. In other examples, the stem region of the hairpin oligonucleotide has a Gibbs free energy (AG) of unfolding under physiological conditions ranging from about -10 kcal/mol to about -50 kcal/mol (e.g., about - 10, -11, -12, -13, -14, -15, -16, -17, -18, -19, -20, -21, -22, -23, -24, -25, -26, -27, -28, -29, -30, -31, -32, -33, -34, -35, -36, -37, -38, -39, -40, -41, -42, -43, -44, -45, -46, -47, -48, -49 or -50 kcal/mol and any range therein). In some examples, the stem region provided herein has a Gibbs free energy (AG) of unfolding under physiological conditions in the range of about -20 kcal/mol to about -40 kcal/mol. In various examples, the stem region provided herein has a Gibbs free energy (AG) of unfolding under physiological conditions of at least about -20 kcal/mol, at least about -25 kcal/mol, at least about -30 kcal/mol or at least about -35 kcal/mol. The term “loop region” refers to a single-stranded region of more than one nucleotide or modified nucleotide that is not base-paired. Suitably, the loop region is of length sufficient to enable formation of the hairpin structure and base pairing of the stem region. According to particular examples, the loop region provided herein is at least about 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 nucleotides, or any range therein, in length. More particularly, the loop region can be about 3 to about 10 nucleotides in length. Even more particularly, the loop region can be about 4 to about 6 nucleotides in length. In certain examples, the loop region is about 4 nucleotides in length. It is contemplated that the loop region may include any suitable sequence of nucleotides (e.g., A, C, G, T and/or U). In various examples, the loop region comprises, consists of or consists essentially of a plurality (e.g., 3, 4, 5, 6, 7 etc) of adenine (A) bases. In one example, the loop region comprises, consists of or consists essentially of a nucleotide sequence of 5'-AAAA-3', or a variant or derivative thereof. The hairpin oligonucleotide herein may include single- and/or double-stranded DNA and/or RNA. In some examples, the hairpin oligonucleotide herein (e.g., the hairpin oligonucleotide of SEQ ID NO: 1 or a hairpin oligonucleotide comprising a binding site of SEQ ID NOs: 3-32) includes single-stranded and double-stranded DNA. In other examples, the hairpin oligonucleotide herein (e.g., the hairpin oligonucleotide of SEQ ID NO: 1 or a hairpin oligonucleotide comprising a binding site of SEQ ID NO: 3-32) includes single-stranded and double-stranded RNA. DNA includes genomic DNA and cDNA. RNA includes mRNA, RNA, RNAi, siRNA, cRNA and autocatalytic RNA. In this regard, the hairpin oligonucleotide may be a DNA-RNA hybrid. A hairpin oligonucleotide of the present disclosure comprises a nucleotide sequence which typically includes nucleotides that comprise an A, G, C, T or U base. However, nucleotide sequences may include other bases such as inosine, methylycytosine, methylinosine, methyladenosine and/or thiouridine, although without limitation thereto. Contemplated herein are “variant” hairpin oligonucleotides that may include, for example, nucleotide sequences of naturally occurring (e.g., allelic) variants and orthologs (e.g., from a different species) of, for example, a binding site, such as an E-box binding site, inclusive of a consensus sequence thereof. As used herein, a nucleic acid “variant” shares a definable nucleotide sequence relationship with a reference nucleic acid sequence (e.g., a hairpin oligonucleotide, a binding/recognition site, SEQ ID NOs:1, 3-32). The “variant” nucleic acid may have one or a plurality of nucleic acids of the reference nucleic acid sequence deleted or substituted by different nucleic acids. It is well understood in the art that some nucleic acids of a DNA/RNA-based binding or recognition site may be substituted or deleted without changing (or only having minimal change to) the affinity of the target protein therefor. Suitably, nucleic acid variants share at least 60% or 65%, 66%, 67%, 68%, 69%, preferably at least 70%, 71%, 72%, 73%, 74% or 75%, more particularly at least 80%, 81%, 82%, 83%, 84%, or 85%, and even more particularly at least 90%, 91%, 92%, 93%, 94%, or 95% nucleotide sequence identity with an isolated nucleic acid of the invention (e.g., SEQ ID NOs: 1, 3 to 32). Percent sequence identity may be determined by any method known in the art, such as that described herein. Terms used generally herein to describe sequence relationships between respective proteins and nucleic acids include “comparison window”, “sequence identity”, “percentage of sequence identity” and “substantial identity”. Because respective nucleic acids/proteins may each comprise (1) only one or more portions of a complete nucleic acid/protein sequence that are shared by the nucleic acids/proteins, and (2) one or more portions which are divergent between the nucleic acids/proteins, sequence comparisons are typically performed by comparing sequences over a “comparison window” to identify and compare local regions of sequence similarity. A “comparison window” refers to a conceptual segment of typically 6, 9 or 12 contiguous residues that is compared to a reference sequence. The comparison window may comprise additions or deletions (i.e., gaps) of about 20% or less as compared to the reference sequence for optimal alignment of the respective sequences. Optimal alignment of sequences for aligning a comparison window may be conducted by computerised implementations of algorithms (Geneworks program by Intelligenetics; GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package Release 7.0, Genetics Computer Group, 575 Science Drive Madison, WI, USA, incorporated herein by reference) or by inspection and the best alignment (i.e., resulting in the highest percentage homology over the comparison window) generated by any of the various methods selected. Reference also may be made to the BLAST family of programs as for example disclosed by Altschul et al., 1997, Nucl. Acids Res. 25 3389, which is incorporated herein by reference. A detailed discussion of sequence analysis can be found in Unit 19.3 of CURRENT PROTOCOLS IN MOLECULAR BIOLOGY Eds. Ausubel et al. (John Wiley & Sons Inc NY, 1995-1999). The term “sequence identity” is used herein in its broadest sense to include the number of exact nucleotide or amino acid matches having regard to an appropriate alignment using a standard algorithm, having regard to the extent that sequences are identical over a window of comparison. Thus, a “percentage of sequence identity” is calculated by comparing two optimally aligned sequences over the window of comparison, determining the number of positions at which the identical nucleic acid base (e.g., A, T, C, G, U) or amino acid residue occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the window of comparison (i.e., the window size), and multiplying the result by 100 to yield the percentage of sequence identity. For example, “sequence identity” may be understood to mean the “match percentage” calculated by the DNASIS computer program (Version 2.5 for windows; available from Hitachi Software engineering Co., Ltd., South San Francisco, California, USA). Also contemplated herein are nucleic acid fragments, such as oligonucleotide fragments. A “fragment” is a segment, domain, portion or region of a nucleic acid, which respectively constitutes less than 100% of the nucleotide sequence. A non-limiting example is an amplification product or a primer or probe. In particular examples, a nucleic acid fragment may comprise, for example, at least 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 55, 60, 65, 70, 75, 80 (inclusive of any range therein) contiguous nucleotides of said nucleic acid (e.g., SEQ ID NO: 1). Further contemplated herein are nucleic acid derivatives, inclusive of oligonucleotide derivatives. Such oligonucleotide derivatives may include, for example, one or more modifications and/or conjugates as described herein. By way of example, the hairpin oligonucleotides may be conjugated to one or more moieties or groups which enhance the activity, cellular distribution or cellular uptake thereof. These moieties or groups may be covalently bound to functional groups such as primary or secondary hydroxyl groups. Exemplary moieties or groups include intercalators, reporter molecules, polyamines, polyamides, polyethylene glycols, polyethers, groups that enhance the pharmacodynamic properties of oligomers, and groups that enhance the pharmacokinetic properties of oligomers. Typical conjugate groups include cholesterols, lipids, phospholipids, biotin, phenazine, folate, phenanthridine, anthraquinone, acridine, fluoresceins, rhodamines, coumarins and dyes/labels (e.g., Cy5 dye to determine cellular uptake and/or localisation of the hairpin oligonucleotide). A hairpin oligonucleotide of the present disclosure suitably does not hybridize to a target or known RNA to reduce translation thereof. In particular examples, the hairpin oligonucleotide does not function as an antisense oligonucleotide (i.e., does not comprise a region that is complementary to at least a portion of a specific mRNA molecule, such as encoding an endogenous polypeptide and capable of interfering with a post-transcriptional event, such as mRNA translation). In other examples, the hairpin oligonucleotide is not, or does not form part of, a stranded oligonucleotide for gene silencing (such as RNA interference; i.e., not a double stranded oligonucleotide for siRNA or shRNA). Additionally, in particular examples, the hairpin oligonucleotide is not, or does not function as, an aptamer oligonucleotide. In alternative examples, however, the hairpin oligonucleotides described herein (e.g., the hairpin oligonucleotide of SEQ ID NO: 1 or a hairpin oligonucleotide comprising a binding site of SEQ ID NO: 3-32) may be considered to comprise or function as an aptamer oligonucleotide (e.g., an RNA aptamer or a DNA aptamer). Accordingly, in particular examples, the hairpin oligonucleotide described herein may comprise a synthetic oligonucleotide sequence. As used herein, a “synthetic oligonucleotide sequence” refers to an oligonucleotide sequence which lacks a corresponding sequence that occurs naturally. By way of example, a synthetic oligonucleotide sequence is not complementary to a specific RNA molecule or portion thereof, such as one encoding an endogenous polypeptide. As such, the synthetic oligonucleotide sequence is suitably not capable of directly interfering with a post-transcriptional event, such as RNA translation. Suitably, the hairpin oligonucleotide is capable of inhibiting or reducing an activity of the target protein. As used herein, the phrase “reduces an activity of the target protein” or the like refers to a hairpin oligonucleotide of the present disclosure reducing the ability of a target protein to exert a biological effect. In relation to transcription factors, this may relate to their ability to contact and/or bind to a DNA sequence, such as a promoter sequence or an enhancer sequence, and modulate (e.g., promote or inhibit) expression of the relevant gene. In particular examples, the activity of the target protein, such as contacting and/or binding a DNA sequence, is less than about 95%, 90%, 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10%, 5%, 2% or 1% of that in the absence of the oligonucleotide. Inhibition of an activity of the target protein by the hairpin oligonucleotide may be assessed by any means known in the art. In the context of transcription factors, this may be assessed by measuring a level of expression of a target gene, whose expression may be at least partly modulated by the target protein, such as at an mRNA and/or protein level (i.e., transcription and/or translation). This can be directly or indirectly achieved by measuring the amount of RNA encoded by the target gene and/or the amount of protein translated from an encoding RNA. In relation to cMyc, this may be assessed by determining an expression level (e.g., mRNA and/or protein) of one or more markers or mediators of the cell cycle (e.g., E2F1, CDK4, CDC25A, p27, p15), apoptosis (e.g., Bax, Mcl-1, Bcl2), cellular proliferation (e.g., MINA53, ID2, PTMA) and/or cellular metabolism (e.g., CAD, LDHA, ODC-1). Additionally, this can be measured indirectly by assessing a level of activation of cell signalling pathways downstream of the target gene or target protein in question. For example, a level of cMyc signalling may be determined by assessing a level of cell cycle activity, apoptotic activity, cellular proliferation and/or cellular metabolism. Typically, a hairpin oligonucleotide of the present disclosure will be synthesized in vitro, such as by chemical synthesis (e.g., solid-phase synthesis). However, in some instances, particularly where modified bases and a modified backbone are not required, they can be expressed in vitro or in vivo in a suitable system, such as by a recombinant virus or cell. Suitably, the hairpin oligonucleotides described herein are isolated. For the purposes of this disclosure, by “isolated” is meant material that has been removed from its natural state or otherwise been subjected to human manipulation. Isolated material, such as the hairpin oligonucleotides, may be substantially or essentially free from components that normally accompany it in its natural state, or may be manipulated so as to be in an artificial state together with components that normally accompany it in its natural state. Isolated material may be in native, chemical synthetic or recombinant form. The binding site for the target protein may be complementary to or comprise the entirety of a consensus or reference sequence thereof, or a part thereof. It is also envisaged that the binding site for the target protein may include a variant of a consensus or reference sequence thereof. In this regard, the degree of identity of the sequence of the binding site to the consensus nucleic acid sequence or the reference nucleic acid sequence of the binding site should be at least 90% (e.g., 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% and any range therein) and more particularly 95-100%. The hairpin oligonucleotide may of course comprise unrelated sequences, such as at a 5’ and/or 3’ end of the consensus or reference nucleic acid sequence, which may function to stabilize the molecule, such as described herein. Suitably, the hairpin oligonucleotide provided herein specifically binds to the target protein or binds to the target protein with high affinity. In some examples, the hairpin oligonucleotide binds to the target protein at an affinity that is at least about 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 150%, 200%, 300%, 400%, 500%, or any range therein, greater than the affinity of a DNA ligand (e.g., an unmodified double stranded DNA molecule) comprising, consisting of or consisting essentially of the binding site (e.g., a binding site of SEQ ID NOs: 3-32) of the hairpin oligonucleotide for the target protein. As used herein, the term “binds” refers to the interaction of the hairpin oligonucleotide with the target protein (e.g., a transcription factor, such as cMyc) and means that the interaction is dependent upon the presence of a particular structure (e.g., a binding site having a particular nucleic acid sequence) on the hairpin oligonucleotide that is recognised by the target protein. For example, and by virtue of the binding site, the hairpin oligonucleotide recognizes and binds to a specific target protein rather than to molecules or proteins generally. As used herein, the term “specifically binds” shall be taken to mean that the binding interaction between a hairpin oligonucleotide disclosed herein and a target protein described herein (e.g., cMyc) is dependent on detection of the target protein by the hairpin oligonucleotide. Accordingly, the hairpin oligonucleotide preferentially binds or recognizes the target protein even when present in a mixture of other molecules, proteins, nucleic acids or organisms. As used herein, the terms “high affinity” and “relatively high affinity” are used interchangeably herein and refer to a binding affinity between a hairpin oligonucleotide and the target protein of interest with a K _D of at least about 10 ^-6 M, more particularly at least about 10 ^-7 M, more particularly at least about 10 ^-8 M, even more particularly at least about 10 ^-9 M and yet even more particularly between about 10 ^-8 M to about 10 ^-10 M. As used herein, the terms “low affinity” and “relatively low affinity” are used interchangeably herein and refer to a binding affinity between a hairpin oligonucleotide and the target protein of interest with a K _D of less than about 10 ^-6 M, preferably less than about 10 ^-5 M, more preferably less than about 10 ^-4 M and even more preferably between about 10 ^-2 M to about 10- ⁴ M. The determination of such affinity may be conducted under standard competitive binding immunoassay procedures, as are known in the art, such as electrophoretic shift assay (EMSA), ELISA and surface plasmon resonance (SPR). Suitably, the hairpin oligonucleotides of the present disclosure inhibit the binding between the target protein and one or more of its binding sites (e.g., a consensus DNA binding site, such as the DNA binding sites of SEQ ID NOs: 3-32). In some examples, the hairpin oligonucleotide has a half maximal inhibitory concentration (IC ₅₀ ) of about 500 nM or less (e.g., about 500 nM or less, about 400 nM or less, about 300 nM or less, about 200 nM or less, about 100 nM or less, about 50 nM or less, about 25 nM or less, about 10 nM or less, about 1 nM or less, etc.) for inhibiting binding of the target protein (e.g., cMyc or cMyc:Max) to a binding site thereof (e.g., 5'-CACGTG-3' or 5'-GAGCACGTGGTT-3'). In other examples, the hairpin oligonucleotide has a half maximal inhibitory concentration (IC50) of between about 1 nM and about 500 nM (e.g., about 1, 5, 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 120, 140, 160, 180, 200, 250, 300, 350, 400, 450, 500 nM or any range therein) for inhibiting binding of the target protein (e.g., cMyc or cMyc:Max) to a binding site thereof (e.g., 5'-CACGTG-3' or 5'- GAGCACGTGGTT-3'). In certain examples, the hairpin oligonucleotide has a half maximal inhibitory concentration (IC ₅₀ ) of about 100 nM or less for inhibiting binding of cMyc to a binding site thereof (e.g., 5'-CACGTG-3' or 5'-GAGCACGTGGTT-3'). In certain examples, the hairpin oligonucleotide has a half maximal inhibitory concentration (IC50) of about 150 nM or less for inhibiting binding of cMyc:Max to a binding site thereof (e.g., 5'-CACGTG-3' or 5'- GAGCACGTGGTT-3'). Methods of measuring the ability of a hairpin oligonucleotide to inhibit binding of a target protein (e.g., human cMyc or cMyc:Max dimer) and a binding site thereof (e.g., 5'-CACGTG-3' or 5'-GAGCACGTGGTT-3') are known in the art, including, without limitation, via EMSA, SPR analysis, ELISA assays, and flow cytometry. Modified Bases Hairpin oligonucleotides of the present disclosure may have nucleobase (“base”) modifications or substitutions. Such modifications can advantageously increase the binding specificity of the stem region for the target protein and/or reduce or minimise the immunogenicity or antigenicity of the hairpin oligonucleotide. In particular examples, one or more bases (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 etc bases inclusive of any range therein) of the oligonucleotide described herein are modified. In certain examples, one or more nucleotides (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 etc nucleotides) at a 5’ end of the hairpin oligonucleotide are modified. In other examples, one or more nucleotides (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 etc nucleotides) at a 3’ end of the hairpin oligonucleotide are modified. In some examples, all bases of the oligonucleotide described herein are modified. In alternative examples, no bases of the oligonucleotide described herein are modified. In certain examples, at least about 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 100% or any range therein of the bases of the hairpin oligonucleotide are modified. Examples of modified bases include oligonucleotides comprising one of the following at the 2' position: OH; F; O-, S-, or N-alkyl; O-, S-, or N-alkenyl; O-, S- or N-alkynyl; or O-alkyl-O- alkyl, wherein the alkyl, alkenyl and alkynyl may be substituted or unsubstituted C1 to C10 alkyl or C2 to C10 alkenyl and alkynyl. In one example, the hairpin oligonucleotide comprises one of the following at the 2' position: O[(CH ₂ )nO]mCH ₃ , O(CH ₂ )nOCH ₃ , O(CH ₂ )nNH ₂ , O(CH2)nCH3, O(CH2)nONH2, and O(CH2)nON[(CH2)nCH3]2, where n and m are from 1 to about 10. Further examples of modified oligonucleotides include one or more nucleotides comprising one of the following at the 2' position: C1 to C10 lower alkyl, substituted lower alkyl, alkenyl, alkynyl, alkaryl, aralkyl, O-alkaryl or O-aralkyl, SH, SCH ₃ , OCN, Cl, Br, CN, CF ₃ , OCF ₃ , SOCH3, SO2CH3, ONO2, NO2, N3, NH2, heterocycloalkyl, heterocycloalkaryl, aminoalkylamino, polyalkylamino, substituted silyl, an RNA cleaving group, a reporter group, an intercalator, a group for improving the pharmacokinetic properties of an oligonucleotide, or a group for improving the pharmacodynamic properties of an oligonucleotide, and other substituents having similar properties. In particular examples, the modification is selected from the group consisting of a 2'-O-methyl, 2'-O-methoxyethoxy, 2'-fluoro, 2'-allyl, 2'-O-[2-(methylamino)-2-oxoethyl], 4'-thio, 4'-CH2- O-2'-bridge, 4'-(CH2)2-O-2'-bridge, 2'-LNA, 2'-amino, fluoroarabinonucleotide, threose nucleic acid or 2'-O--(N-methlycarbamate). In some examples, the modified base comprises a 2'-O-methyl, 2'-fluoro, 2'-allyl, 2'-O-[2-(methylamino)-2-oxoethyl], 4'-thio, 4'-CH2-O-2'- bridge, 4'-(CH2)2-O-2'-bridge, 2'-amino, fluoroarabinonucleotide, threose nucleic acid, 2'-O-- (N-methlycarbamate) and any combination thereof. Suitably, the modification includes 2'-methoxy (2'-O-CH3 or 2’OMe), that is, an alkoxyalkoxy group. In certain examples, the hairpin oligonucleotide includes one or more nucleotides (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 etc nucleotides) at a 5’ end and/or a 3’ thereof that are 2’OMe modified. In particular examples, the hairpin oligonucleotide includes at least one nucleotide at a 5’ end and a 3’ thereof that are 2’OMe modified. In some examples, the hairpin oligonucleotide includes at least one nucleotide at a 5’ end thereof that is 2’OMe modified. In other examples, the hairpin oligonucleotide includes at least one nucleotide at a 3’ end thereof that is 2’OMe modified. In other examples, the modification includes 2'-methoxyethoxy (2'-O-CH2CH2OCH3 (also known as 2'-O-(2-methoxyethyl) or 2'-MOE) (Martin et al., 1995). In further examples, the modification includes 2'-dimethylaminooxyethoxy, that is, a O(CH2)2ON(CH3)2 group (also known as 2'-DMAOE), or 2'-dimethylaminoethoxyethoxy (also known in the art as 2'-O- dimethyl-amino-ethoxy-ethyl or 2'-DMAEOE), that is, 2'-O-CH ₂ -O-CH ₂ -N(CH ₃ ) ₂ . Other modifications include 2'-aminopropoxy (2'-OCH2CH2CH2NH2), 2'-allyl (2'-CH2-CH=CH2), 2'- O-allyl (2'-O-CH ₂ -CH=CH ₂ ) and 2'-fluoro (2'-F). The 2'-modification may be in the arabino (up) position or ribo (down) position. In certain examples, a 2'-arabino modification is 2'-F. Similar modifications may also be made at other positions on the oligonucleotide, particularly the 3' position of the sugar on the 3' terminal nucleotide or in 2'-5' linked oligonucleotides and the 5' position of the 5' terminal nucleotide. Oligonucleotides may also have sugar mimetics, such as cyclobutyl moieties in place of the pentofuranosyl sugar. Representative United States patents that teach the preparation of such modified sugar structures include, but are not limited to, US 4,981,957, US 5,118,800, US 5,319,080, US 5,359,044, US 5,393,878, US 5,446,137, US 5,466,786, US 5,514,785, US 5,519,134, US 5,567,811, US 5,576,427, US 5,591,722, US 5,597,909, US 5,610,300, US 5,627,053, US 5,639,873, US 5,646,265, US 5,658,873, US 5,670,633, US 5,792,747, and US 5,700,920. A further modification of the sugar includes Locked Nucleic Acids (LNAs) in which the 2'- hydroxyl group is linked to the 3' or 4' carbon atom of the sugar ring, thereby forming a bicyclic sugar moiety. In one example, the linkage is a methylene (-CH2-)n group bridging the 2' oxygen atom and the 4' carbon atom, wherein n is 1 or 2. LNAs and preparation thereof are described in WO 98/39352 and WO 99/14226. Modified nucleobases include other synthetic and natural nucleobases such as, for example, 5- methylcytosine (5-me-C), 5-hydroxymethyl cytosine, xanthine, hypoxanthine, 2- aminoadenine, 6-methyl and other alkyl derivatives of adenine and guanine, 2-propyl and other alkyl derivatives of adenine and guanine, 2-thiouracil, 2-thiothymine and 2-thiocytosine, 5- halouracil and cytosine, 5-propynyl (-CC-CH3) uracil and cytosine and other alkynyl derivatives of pyrimidine bases, 6-azo uracil, cytosine and thymine, 5-uracil (pseudouracil), 4- thiouracil, 8-halo, 8-amino, 8-thiol, 8-thioalkyl, 8-hydroxyl and other 8-substituted adenines and guanines, 5-halo particularly 5-bromo, 5-trifluoromethyl and other 5-substituted uracils and cytosines, 7-methylguanine and 7-methyladenine, 2-F-adenine, 2-amino-adenine, 8- azaguanine and 8-azaadenine, 7-deazaguanine and 7-deazaadenine and 3-deazaguanine and 3- deazaadenine, m ¹ A(1-methyladenosine); m ² A(2-methyladenosine); Am (2’-O- methyladenosine); ms ² m ⁶ A(2-methylthio-N ⁶ -methyladenosine); i ⁶ A (N ⁶ - isopentenyladenosine); ms ² i ⁶ A(2-methylthio-N ⁶ isopentenyladenosine); io ⁶ A(N ⁶ -(cis- hydroxyisopentenyl)adenosine); ms ² io ⁶ A(2-methylthio-N ⁶ -(cis- hydroxyisopentenyl)adenosine); g ⁶ A(N6-glycinylcarbamoyladenosine); t ⁶ A(N ⁶ - threonylcarbamoyladenosine); ms ² t ⁶ A(2-methylthio-N ⁶ -threonyl carbamoyladenosine); m ⁶ t ⁶ A(N ⁶ -methyl-N ⁶ -threonylcarbamoyladenosine); hn ⁶ A(N ⁶ - hydroxynorvalylcarbamoyladenosine); ms ² hn ⁶ A(2-methylthio-N ⁶ -hydroxynorvalyl carbamoyladenosine); Ar(p)(2’-O-ribosyladenosine(phosphate)); I (inosine); m ¹ I(1- methylinosine); m ¹ Im(1,2’-O-dimethylinosine); m ³ C(3-methylcytidine); Cm(2’-O- methylcytidine); s ² C(2-thiocytidine); ac ⁴ C(N ⁴ -acetylcytidine); (5-formylcytidine); m ⁵ Cm(5,2’-O-dimethylcytidine); ac ⁴ Cm(N ⁴ -acetyl-2’-O-methylcytidine); k ² C(lysidine); m ¹ G(1-methylguanosine); m ² G(N ² -methylguanosine); m ⁷ G(7-methylguanosine); Gm(2’-O- methylguanosine); m ² 2G(N2,N2-dimethylguanosine); m ² Gm(N ² ,2’-O-dimethylguanosine); m ² ₂ Gm(N ² ,N ² ,2’-O-trimethylguanosine); Gr(p)(2’-O-ribosylguanosine (phosphate)); yW (wybutosine); o ² yW (peroxywybutosine); OHyW (hydroxywybutosine); OHyW* (undermodified hydroxywybutosine); imG (wyosine); mimG (methylwyosine); Q (queuosine); oQ (epoxyqueuosine); galQ (galactosyl-queuosine); manQ (mannosyl-queuosine); preQo (7- cyano-7-deazaguanosine); preQ ₁ (7-aminomethyl-7-deazaguanosine); G ⁺ (archaeosine); D (dihydrouridine); m ⁵ Um(5,2’-O-dimethyluridine); s ⁴ U(4-thiouridine); m ⁵ s ² U(5-methyl-2- thiouridine); s ² Um(2-thio-2’-O-methyluridine); acp ³ U(3-(3-amino-3-carboxypropyl)uridine); ho ⁵ U(5-hydroxyuridine); mo ⁵ U(5-methoxyuridine); cmo ⁵ U(uridine 5-oxyacetic acid); mcmo ⁵ U (uridine 5-oxyacetic acid methyl ester); chm ⁵ U(5-(carboxyhydroxymethyl)uridine)); mchm ⁵ U(5-(carboxyhydroxymethyl)uridine methyl ester); mcm ⁵ U(5- methoxycarbonylmethyluridine); mcm ⁵ Um(5-methoxycarbonylmethyl-2’-O-methyluridine); mcm ⁵ s ² U(5-methoxycarbonylmethyl-2-thiouridine); nm ⁵ s ² U(5-aminomethyl-2-thiouridine); mnm ⁵ U(5-methylaminomethyluridine); mnm ⁵ s ² U(5-methylaminomethyl-2-thiouridine); mnm ⁵ se ² U(5-methylaminomethyl-2-selenouridine); ncm ⁵ U(5-carbamoylmethyluridine); ncm ⁵ Um(5-carbamoylmethyl-2’-O-methyluridine); cmnm ⁵ U(5- carboxymethylaminomethyluridine); cmnm ⁵ Um(5-carboxymethylaminomethyl-2’-O- methyluridine); cmnm ⁵ s ² U(5-carboxymethylaminomethyl-2-thiouridine); m ⁶ 2A(N ⁶ ,N ⁶ - dimethyladenosine); Im(2’-O-methylinosine); m ⁴ C(N4-methylcytidine); m ⁴ Cm(N ⁴ ,2’-O- dimethylcytidine); hm ⁵ C(5-hydroxymethylcytidine); m ³ U(3-methyluridine); cm ⁵ U(5- carboxymethyluridine); m ⁶ Am(N ⁶ ,2’-O-dimethyladenosine); m ⁶ 2Am (N ⁶ ,N ⁶ ,O-2’- trimethyladenosine); m ^2,7 G(N2,7-dimethylguanosine); m ^2,2,7 G(N2,N2,7-trimethylguanosine); m ³ Um(3,2’-O-dimethyluridine); m ⁵ D(5-methyldihydrouridine); f ⁵ Cm (5-formyl-2’-O- methylcytidine); m ¹ Gm (1,2’-O-dimethylguanosine); m ¹ Am(1,2’-O-dimethyladenosine); τm ⁵ U(5-taurinomethyluridine); τm ⁵ s ² U(5-taurinomethyl-2-thiouridine)); imG-14 (4- demethylwyosine); imG2(isowyosine); or ac ⁶ A(N ⁶ -acetyladenosine). Further modified nucleobases include tricyclic pyrimidines, such as phenoxazine cytidine (1H- pyrimido[5,4-b][1,4]benzoxazin-2(3H)-one), and phenothiazine cytidine (1H-pyrimido[5,4- b][1,4]benzothiazin-2(3H)-one), G-clamps such as, for example, a substituted phenoxazine cytidine (e.g., 9-(2-aminoethoxy)-H-pyrimido[5,4-b][1,4]benzoxazin-2(3H)-one ), carbazole cytidine (2H-pyrimido[4,5-b]indol-2-one), and pyridoindole cytidine (H- pyrido[3',2':4,5]pyrrolo[2,3-d]pyrimidin-2-one). Modified nucleobases may also include those in which the purine or pyrimidine base is replaced with other heterocycles, for example, 7-deaza-adenine, 7-deazaguanosine, 2- aminopyridine and 2-pyridone. Further nucleobases include those disclosed in US 3,687,808, those disclosed in J.I. Kroschwitz (editor), The Concise Encyclopedia of Polymer Science and Engineering, pages 858-859, John Wiley and Sons (1990), those disclosed by Englisch et al. (1991), and those disclosed by Y.S. Sanghvi, Chapter 15: Antisense Research and Applications, pages 289-302, S.T. Crooke, B. Lebleu (editors), CRC Press, 1993. Certain of these nucleobases are particularly useful for increasing the binding affinity of the hairpin oligonucleotide. These include 5-substituted pyrimidines, 6-azapyrimidines and N-2, N-6 and O-6 substituted purines, including 2-aminopropyladenine, 5-propynyluracil and 5- propynylcytosine. 5-methylcytosine substitutions have been shown to increase nucleic acid duplex stability by 0.6-1.2 ^o C. In certain examples, these nucleobase substitutions are combined with 2'-O-methoxyethyl sugar modifications. Representative United States patents that teach the preparation of certain of the above noted modified nucleobases as well as other modified nucleobases include, but are not limited to, US 3,687,808, US 4,845,205, US 5,130,302, US 5,134,066, US 5,175,273, US 5,367,066, US 5,432,272, US 5,457,187, US 5,459,255, US 5,484,908, US 5,502,177, US 5,525,711, US 5,552,540, US 5,587,469, US 5,594,121, US 5,596,091, US 5,614,617, US 5,645,985, US 5,830,653, US 5,763,588, US 6,005,096, US 5,681,941 and US 5,750,692. Unless stated to the contrary, reference to an A, T, G, U or C base herein can either mean a naturally occurring base or a modified version thereof. Backbones Oligonucleotides of the present disclosure include those having modified backbones or non- natural internucleotide linkages. Oligonucleotides having modified backbones include those that retain a phosphorus atom in the backbone and those that do not have a phosphorus atom in the backbone. Such modifications, inclusive of a phosphorothioate backbone, may advantageously protect the hairpin oligonucleotide from digestion by nucleases and/or increase the affinity of the hairpin oligonucleotide to the target protein. This increased affinity may be due, at least in part, to additional electrostatic and London forces. Modified oligonucleotide backbones containing a phosphorus atom therein include, for example, phosphorothioates, chiral phosphorothioates, phosphorodithioates, phosphotriesters, aminoalkylphosphotriesters, methyl and other alkyl phosphonates including 3'-alkylene phosphonates, 5'-alkylene phosphonates and chiral phosphonates, phosphinates, phosphoramidates including 3'-amino phosphoramidate and aminoalkylphosphoramidates, thionophosphoramidates, thionoalkylphosphonates, thionoalkylphosphotriesters, selenophosphates, and boranophosphates having normal 3'-5' linkages, 2'-5' linked analogs of these, and those having inverted polarity wherein one or more internucleotide linkages is a 3' to 3', 5' to 5' or 2' to 2' linkage. Oligonucleotides having inverted polarity comprise a single 3' to 3' linkage at the 3'-most internucleotide linkage, that is, a single inverted nucleoside residue which may be abasic (the nucleobase is missing or has a hydroxyl group in place thereof). Various salts, mixed salts and free acid forms are also included. Representative United States patents that teach the preparation of the above phosphorus- containing linkages include, but are not limited to, US 3,687,808, US 4,469,863, US 4,476,301, US 5,023,243, US 5,177,196, US 5,188,897, US 5,264,423, US 5,276,019, US 5,278,302, US 5,286,717, US 5,321,131, US 5,399,676, US 5,405,939, US 5,453,496, US 5,455,233, US 5,466,677, US 5,476,925, US 5,519,126, US 5,536,821, US 5,541,306, US 5,550,111, US 5,563,253, US 5,571,799, US 5,587,361, US 5,194,599, US 5,565,555, US 5,527,899, US 5,721,218, US 5,672,697 and US 5,625,050. Modified oligonucleotide backbones that do not include a phosphorus atom therein include, for example, backbones formed by short chain alkyl or cycloalkyl internucleoside linkages, mixed heteroatom and alkyl or cycloalkyl internucleoside linkages, or one or more short chain heteroatomic or heterocyclic internucleoside linkages. These include those having morpholino linkages (formed in part from the sugar portion of a nucleoside); siloxane backbones; sulfide, sulfoxide and sulfone backbones; formacetyl and thioformacetyl backbones; methylene formacetyl and thioformacetyl backbones; riboacetyl backbones; alkene containing backbones; sulfamate backbones; methyleneimino and methylenehydrazino backbones; sulfonate and sulfonamide backbones; amide backbones; and others having mixed N, O, S and CH2 component parts. Representative United States patents that teach the preparation of the above oligonucleotides include, but are not limited to, US 5,034,506, US 5,166,315, US 5,185,444, US 5,214,134, US 5,216,141, US 5,235,033, US 5,264,562, US 5,264,564, US 5,405,938, US 5,434,257, US 5,466,677, US 5,470,967, US 5,489,677, US 5,541,307, US 5,561,225, US 5,596,086, US 5,602,240, US 5,610,289, US 5,602,240, US 5,608,046, US 5,610,289, US 5,618,704, US 5,623,070, US 5,663,312, US 5,633,360, US 5,677,437, US 5,792,608, US 5,646,269 and US 5,677,439. Suitably, the hairpin oligonucleotide described herein at least partly comprises a modified backbone. Exemplary modified backbones useful for the invention can include those which comprise a phosphorothioate, a non-bridging oxygen atom substituting a sulfur atom, a phosphonate such as a methylphosphonate, a phosphodiester, a phosphoromorpholidate, a phosphoropiperazidate, amides, methylene(methylamino), fromacetal, thioformacetal, a peptide nucleic acid or a phosphoroamidate such as a morpholino phosphorodiamidate (PMO), N3’-P5’ phosphoramidite or thiophosphoroamidite. In particular examples, the oligonucleotide comprises a 5’ region comprising one or more bases which are modified and/or which have a modified backbone and a 3’ region comprising one or more bases which are modified and/or which have a modified backbone. In some examples, all internucleotide linkages of the hairpin oligonucleotide described herein are modified or comprise a modification, such as a phosphorothioate modification. In alternative examples, no internucleotide linkages of the hairpin oligonucleotide described herein are modified or comprise a modification. In particular examples, the hairpin oligonucleotide comprises one or a plurality of phosphorothioate internucleotide linkages. More particularly, all internucleotide linkages of the hairpin oligonucleotide comprise a phosphorothioate modification. In certain examples, at least about 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 100% or any range therein of the internucleotide linkages of the hairpin oligonucleotide are modified or non-natural. In particular examples, at least a portion of the oligonucleotide has/is a ribonucleic acid, deoxyribonucleic acid, a DNA phosphorothioate, an RNA phosphorothioate, 2'-O-methyl- oligonucleotide, 2'-O-methyl-oligodeoxyribonucleotide, 2'-O-hydrocarbyl ribonucleic acid, 2'- O-hydrocarbyl DNA, 2'-O-hydrocarbyl RNA phosphorothioate, 2'-O-hydrocarbyl DNA phosphorothioate, 2'-F-phosphorothioate, 2'-F-phosphodiester, 2'-methoxyethyl phosphorothioate, 2-methoxyethyl phosphodiester, deoxy methylene(methylimino) (deoxy MMI), 2'-O-hydrocarby MMI, deoxy-methylphos-phonate, 2'-O-hydrocarbyl methylphosphonate, morpholino, 4'-thio DNA, 4'-thio RNA, peptide nucleic acid, 3'-amidate, deoxy 3'-amidate, 2'-O-hydrocarbyl 3'-amidate, locked nucleic acid, cyclohexane nucleic acid, tricycle-DNA, 2'fluoro-arabino nucleic acid, N3'-P5' phosphoroamidate, carbamate linked, phosphotriester linked, a nylon backbone modification and any combination thereof. Methods of treating disease associated with a target protein The present inventors have also surprising shown that the hairpin oligonucleotides described herein can be utilised to bind the target protein, such as a transcription factor, in cells and thereby inhibit a biological activity thereof. As such, the hairpin oligonucleotides may be administered to a subject in need thereof to prevent a disease, disorder or condition associated with or dependent on increased activity and/or expression of the target protein. Therefore, in one form, the present disclosure provides a method of inhibiting a target protein of a cell, said method including the step of contacting the cell with an effective amount the hairpin oligonucleotide described herein. In a related form, the present disclosure provides for the use of the hairpin oligonucleotide or the pharmaceutical composition provided herein in the manufacture of a medicament for inhibiting a target protein of a cell. In another related form, the present disclosure provides a hairpin oligonucleotide or a pharmaceutical composition described herein for use in inhibiting a target protein of a cell. It is contemplated that such methods may be performed in relation to cells in vitro, in vivo and/or ex vivo. In some examples, the method is performed in vitro, such as with cancer cells or patient-derived xenografts isolated from a subject, an organoid or a stem cell-derived (e.g., induced pluripotent stem cell(iPSC)-derived) cell, as described herein. Accordingly, in some examples, the present method includes the earlier step of isolating the cells expressing the target protein from a subject. In other examples, the present method is performed in vivo in a subject. As used herein, the term “effective amount” and the like refers to an amount of the hairpin oligonucleotide or the pharmaceutical composition that is sufficient to induce a desired physiological outcome (e.g., at least partly inhibiting a target protein’s activity). An effective amount can be administered in one or more administrations, applications or dosages. Such delivery is dependent on a number of variables including the time period which the individual dosage unit is to be used, the bioavailability of the composition, the route of administration, etc. In another form, the present disclosure provides a method of preventing, ameliorating or treating a disease, disorder or condition associated with a target protein in a subject, said method including the step of administering to the subject a therapeutically effective amount of the hairpin oligonucleotide or the pharmaceutical composition described herein to thereby prevent, ameliorate or treat the disease, disorder or condition. In a related form, the present disclosure also provides for the use of the hairpin oligonucleotide or the pharmaceutical composition described herein in the manufacture of a medicament for preventing, ameliorating or treating a disease, disorder or condition associated with a target protein in a subject. In a further related form, the present disclosure also provides for a hairpin oligonucleotide or a pharmaceutical composition described herein for use in preventing, ameliorating or treating a disease, disorder or condition associated with a target protein in a subject. With respect to the aspects described herein, the term “subject”, “patient” and “individual” includes, but is not limited to, mammals, inclusive of humans, performance animals (such as horses, camels, greyhounds), livestock (such as cows, sheep, horses) and companion animals (such as cats and dogs). Suitably, the subject is a human. In some examples, the subject is a female human. In other examples, the subject is a male human. As used herein, “treating”, “treat” or “treatment” refers to a therapeutic intervention that at least partly ameliorates, eliminates or reduces a symptom or pathological sign of a disease, disorder or condition after it has begun to develop. Treatment need not be absolute to be beneficial to the subject. The beneficial effect can be determined using any methods or standards known to the ordinarily skilled artisan. As used herein, “preventing”, “prevent” or “prevention” refers to a course of action initiated before the onset of a symptom or pathological sign of the disease, disorder or condition, so as to reduce the symptom or pathological sign. It is to be understood that such preventing need not be absolute to be beneficial to a subject. A “prophylactic” treatment is a treatment administered to a subject who does not exhibit signs of the disease, disorder or condition, or exhibits only early signs for the purpose of decreasing the risk of developing a symptom or pathological sign of the disease, disorder or condition. The term “ameliorating” as used herein refers to any improvement in the disease state of a patient suffering from the disease, disorder or condition described herein by administering to a subject in need thereof a hairpin oligonucleotide according to the present disclosure. Such an improvement may also be seen as a slowing or stopping of the progression of the disease, disorder or condition in the subject. Hairpin oligonucleotides of the present disclosure can be used to target any protein of interest that binds or interacts with a particular nucleic acid sequence, inclusive of secondary, tertiary and quaternary structures formed thereby. The target protein may be extracellularly expressed or may be intracellularly expressed. Typically, the hairpin oligonucleotide is used to modify a trait of an animal, more typically to treat or prevent a disease, disorder or condition. In some examples, the disease, disorder or condition will benefit from inhibition of the target protein following administration of the hairpin oligonucleotide. To this end, the disease, disorder or condition may be at least partly caused by an increased expression and/or activity of the target protein (e.g., increased expression and/or activity of cMyc). Diseases, disorders and conditions, which can be treated or prevented using a hairpin oligonucleotide of the present disclosure include, but are not limited, to cancer (for example breast cancer, ovarian cancer, cancers of the central nervous system, gastrointestinal cancer, bladder cancer, skin cancer, lung cancer, head and neck cancers, haematological and lymphoid cancers, bone cancer) rare genetic diseases, neuromuscular and neurological diseases (for example, spinal muscular atrophy, Amyotrophic Lateral Sclerosis, Duchenne muscular dystrophy, Huntington’s disease, Batten disease, Parkinson’s disease, amyotrophic lateral sclerosis, Ataxia-telangiectasia, cerebral palsy) viruses (for example, cytomegalovirus, hepatitis C virus, Ebola haemorrhagic fever virus, human immunodeficiency virus, coronaviruses), cardiovascular disease (for example, familial hypercholesterolemia, hypertriglyceridemia), autoimmune and inflammatory diseases (for example arthritis, lupus, pouchitis, psoriasis, asthma), and non-alcoholic and alcoholic fatty liver diseases. According to particular examples, the disease, disorder or condition is a cancer. Cancers may include any aggressive or potentially aggressive cancers, tumours or other malignancies such as listed in the NCI Cancer Index at http://www.cancer.gov/types, including all major cancer forms such as sarcomas, carcinomas, lymphomas, leukaemias and blastomas, although without limitation thereto. These may include solid cancers and haematological cancers, and more particularly breast cancer, lung cancer inclusive of lung adenocarcinoma, cancers of the reproductive system inclusive of ovarian cancer, cervical cancer, uterine cancer and prostate cancer, cancers of the brain and nervous system, head and neck cancers, gastrointestinal cancers inclusive of colon cancer, colorectal cancer and gastric cancer, liver cancer, kidney cancer, skin cancers such as melanoma and skin carcinomas, blood cell cancers inclusive of lymphoid cancers and myelomonocytic cancers, cancers of the endocrine system such as pancreatic cancer and pituitary cancers, musculoskeletal cancers inclusive of bone and soft tissue cancers, although without limitation thereto. It is contemplated that the cancer can be a breast cancer, which may include any aggressive breast cancers and cancer subtypes known in the art, such as triple negative breast cancer, grade 2 breast cancer, grade 3 breast cancer, lymph node positive (LN+) breast cancer, HER2 positive (HER2+) breast cancer, PR negative (PR-) breast cancer, PR positive (PR ⁺ ) breast cancer, ER negative (ER-) breast cancer and ER positive (ER+) breast cancer. In various examples, the breast cancer is or comprises triple negative breast cancer. The term “therapeutically effective amount” describes a quantity of a specified agent, such as a hairpin oligonucleotide or a composition described herein, sufficient to achieve a desired effect in a subject being treated with that agent or composition. For example, this can be the amount of a hairpin oligonucleotide and optionally one or more further therapeutic agents, necessary to reduce, alleviate and/or prevent a disease, disorder or condition associated with the target protein in question. Suitably, a “therapeutically effective amount” is sufficient to reduce or eliminate a symptom of such a disease, disorder or condition. More particularly, a “therapeutically effective amount” may be an amount sufficient to achieve a desired biological effect, for example an amount that is effective to decrease or prevent disease progression, such as progressive vision loss and blindness. Ideally, a therapeutically effective amount of an agent is an amount sufficient to induce the desired result without causing a substantial cytotoxic effect in the subject. The effective amount of an agent useful for reducing, alleviating and/or preventing the diseases, disorders and conditions described herein will be dependent on the subject being treated, the type and severity of any associated disease, disorder and/or condition (e.g., disease progression), and the manner of administration of the therapeutic composition. Suitably, the methods described herein further include the step of administering a further therapeutic agent to the subject (i.e., in addition to the hairpin oligonucleotide). As such, the hairpin oligonucleotide may be administered alone (i.e., monotherapy) or alternatively be administered in combination with the further therapeutic agent (e.g., a further anti-cancer agent) which aims to treat or prevent a disease, disorder or condition described herein. In certain examples, the hairpin oligonucleotide described herein may be co-administered with (simultaneously or sequentially) a further treatment of a cancer (e.g., an anti-cancer agent). Non-limiting examples of such treatments include drug therapy, chemotherapy, antibody, nucleic acid and other biomolecular therapies, radiation therapy, surgery, nutritional therapy, relaxation or meditational therapy and other natural or holistic therapies, although without limitation thereto. Generally, drugs, biomolecules (e.g., antibodies, inhibitory nucleic acids such as siRNA) or chemotherapeutic agents are referred to herein as “anti-cancer therapeutic agents” or “anti-cancer agents”. Suitably, the treatment is or comprises one or more of chemotherapy, radiation therapy, molecularly targeted therapy and immunotherapy. As such, in particular examples, the present methods further include the step of administering a therapeutically effective amount of an anti-cancer agent to the subject. The methods of the present disclosure may further include the earlier or initial step of identifying the presence of the disease, disorder or condition associated with the target protein in the subject. Similarly, the methods described herein may include the earlier or initial step of identifying a cancer or a cancer cell as a target protein-dependent cancer or cancer cell. Accordingly, the methods of this disclosure may include the initial step of determining an activity level and/or an expression level of the target protein of a cancer cell or the subject’s cancer, such as from a sample (e.g., a biopsy sample or a biological sample) obtained from the subject or the subject’s cancer. Such a determining step may be performed by any means or method of testing known in the art. Target proteins As used herein, a “target”, such as a “target protein” or “target polypeptide”, refers to a molecule upon which a hairpin oligonucleotide of the invention directly or indirectly exerts its effects (e.g., specifically binds or contacts). Typically, the hairpin oligonucleotide of the present disclosure or a portion thereof and the target protein, or a portion thereof, are able to bind under physiological conditions. By “protein” is meant an amino acid polymer. The amino acids may be natural or non-natural amino acids, D- or L-amino acids, as are well understood in the art. A “peptide” is generally referred to as a protein typically having no more than fifty (50) amino acids and a polypeptide is generally referred to as a protein typically having more than fifty (50) amino acids. It is envisaged that the target protein may be a nucleic acid binding protein that can specifically bind to a certain nucleic acid sequence. In particular examples, the target protein is a DNA- binding protein. In other examples, the target protein is an RNA-binding protein. In further examples, the target protein is capable of binding both DNA and RNA. Conventional methods for detecting nucleic acid binding proteins, such as transcription factors, include electrophoretic shift assay (EMSA), supershift EMSA, and ELISA-based techniques. A nucleic acid binding protein may be a complex of two or more individual molecules (e.g., cMyc:Max). Such complexes are commonly referred to as “homodimers”, “heterodimers”, “homotype complexes” and “heterotype complexes”. Such a complex suitably comprises a number of individual components joined together by covalent bonds or non-covalent interactions. Given their well-known ability to bind DNA, it is envisaged that the target protein may be a transcription factor that is capable of binding or specifically binding, such as with high affinity, to the binding site of the hairpin oligonucleotide. As such, the hairpin oligonucleotide can inhibit transcription factor function, for example, by interfering with binding thereof to DNA. The term “transcription factor” as used herein means a protein that possesses a biological function that includes regulation, such as initiation or inhibition/repression, of the transcription of one or more genes. That is, a transcription factor is a protein that possesses a DNA-binding domain (DBD) that allows the protein to bind a specific sequence of DNA (e.g., an enhancer element or promoter sequence). Upon binding the enhancer or promoter element, the transcription factor's presence can aid in initiation of transcription by stabilizing transcription initiation complex formation and/or activity, for example. Transcription factors can also inhibit transcription by blocking (i.e., a repressor) the recruitment of RNA polymerase to one or more specific genes, such as by binding to a silencer sequence. Transcription factors also bind to regulatory DNA sequences, such as enhancer sequences, that can be many hundreds of base pairs downstream or upstream from the transcribed gene. Transcription factors can perform the transcription controlling function either alone or in combination with other proteins, such as by forming an activation complex, and can aid in recruiting RNA polymerase and related proteins to the transcription initiation start site. In view of the above, the binding site of the hairpin oligonucleotide may be or comprise a regulatory DNA sequence, such as a promoter sequence, a silencer sequence or an enhancer sequence, or a fragment or variant thereof. The term “promoter sequence” refers to a polynucleotide region comprising a DNA regulatory sequence, wherein the regulatory sequence is derived from a gene which is capable of binding RNA polymerase and initiating transcription of a downstream (3’-direction) coding sequence. As used herein, the term “enhancer sequence” refers to a sequence capable of increasing gene expression. Such sequences may be located upstream, intronically or downstream of the region to be transcribed. Enhancement of gene expression by enhancer sequences can be achieved through a variety of mechanisms including, but not limited to, increased transcription efficiency, stabilization of mature mRNA, and translation enhancement. The term “silencer sequence” refers to a polynucleotide region comprising a DNA regulatory sequence comprising one or more sequence-specific binding sites for a repressive transcription factor or repressor that can suppress or inhibit transcription from an otherwise active promoter. The binding site of the hairpin oligonucleotide may include one or more additional nucleotides (e.g., 1, 2, 3, 4, 5, etc nucleotides) either side (i.e., 5’ or 3’ end) thereof that are naturally or normally found in a genomic sequence that includes said binding site. Such flanking nucleotide sequences may assist in improving the affinity of the target protein for the binding site. It is further contemplated that the loop region may at least in part facilitate binding of the target protein to the hairpin oligonucleotide. In this regard, the loop region may include a portion, such as a 5’ end or a 3’ end, of the binding site in question. In other examples, the loop region together with the stem region forms a secondary structure that is capable of binding or interacting with a target protein Transcription factors include a wide number of proteins, excluding RNA polymerase, that initiate and regulate the transcription of genes. Exemplary transcription factors include, but are not limited to, AAF, ab1, ADA2, ADA-NF1, AF-1, AFP1, AhR, AIIN3, ALL-1, alpha-CBF, alpha-CP1, alpha-CP2a, alpha-CP2b, alphaHo, alphaH2-alphaH3, Alx-4, aMEF-2, AML1, AML1a, AML1b, AML1c, AML1DeltaN, AML2, AML3, AML3a, AML3b, AMY-1 L, A-Myb, ANF, AP-1, AP-2alphaA, AP-2alphaB, AP- 2beta, AP-2gamma, AP-3 (1), AP-3 (2), AP-4, AP-5, APC, AR, AREB6, Arnt, Arnt (774 M form), ARP-1, ATBF1-A, ATBF1-B, ATF, ATF-1, ATF-2, ATF-3, ATF-3deltaZIP, ATF-a, ATF-adelta, ATPF1, Barhl1, Barhl2, Barx1, Barx2, Bcl-3, BCL-6, BD73, beta-catenin, Bin1, B-Myb, BP1, BP2, brahma, BRCA1, Brn-3a, Brn-3b, Brn-4, BTEB, BTEB2, B-TFIID, C/EBPalpha, C/EBPbeta, C/EBPdelta, CACCbinding factor, Cart-1, CBF (4), CBF (5), CBP, CCAAT-binding factor, CCMT-binding factor, CCF, CCG1, CCK-1a, CCK-1b, CD28RC, cdk2, cdk9, Cdx-1, CDX2, Cdx-4, CFF, Chx10, CLIM1, CLIM2, CNBP, CoS, COUP, CP1, CP1A, CP1C, CP2, CPBP, CPE binding protein, CREB, CREB-2, CRE-BP1, CRE-BPa, CREMalpha, CRF, Crx, CSBP-1, CTCF, CTF, CTF-1, CTF-2, CTF-3, CTF-5, CTF-7, CUP, CUTL1, Cx, cyclin A, cyclin T1, cyclin T2, cyclin T2a, cyclin T2b, DAP, DAX1, DB1, DBF4, DBP, DbpA, DbpAv, DbpB, DDB, DDB-1, DDB-2, DEF, deltaCREB, deltaMax, DF-1, DF- 2, DF-3, Dlx-1, Dlx-2, Dlx-3, DIx4 (long isoform), Dlx-4 (short isoform, Dlx-5, Dlx-6, DP-1, DP-2, DSIF, DSIF-p14, DSIF-p160, DTF, DUX1, DUX2, DUX3, DUX4, E, E12, E2F, E2F+E4, E2F+p107, E2F-1, E2F-2, E2F-3, E2F-4, E2F-5, E2F-6, E47, E4BP4, E4F, E4F1, E4TF2, EAR2, EBP-80, Ebola viral protein 30 (Ebola virus VP30), EC2, EF1, EF-C, EGR1, EGR2, EGR3, EIIaE-A, EIIaE-B, EIIaE-Calpha, EIIaE-Cbeta, EivF, EIf-1, EIk-1, Emx-1, Emx-2, Emx-2, En-1, En-2, ENH-bind. prot., ENKTF-1, EPAS1, epsilonF1, ER, Erg-1, Erg- 2, ERR1, ERR2, ETF, Ets-1, Ets-1 delta Vil, Ets-2, Evx-1, F2F, factor 2, Factor name, FBP, f- EBP, FKBP59, FKHL18, FKHRL1P2, Fli-1, Fos, FOXB1, FOXC1, FOXC2, FOXD1, FOXD2, FOXD3, FOXD4, FOXE1, FOXE3, FOXF1, FOXF2, FOXG1a, FOXG1b, FOXG1c, FOXH1, FOXI1, FOXJ1a, FOXJ1b, FOXJ2 (long isoform), FOXJ2 (short isoform), FOXJ3, FOXK1a, FOXK1b, FOXK1c, FOXL1, FOXM1a, FOXM1b, FOXM1c, FOXN1, FOXN2, FOXN3, FOX01a, FOX01b, FOXO2, FOXO3a, FOXO3b, FOXO4, FOXP1, FOXP3, Fra-1, Fra-2, FTF, FTS, G factor, G6 factor, GABP, GABP-alpha, GABP-beta1, GABP-beta2, GADD 153, GAF, gammaCMT, gammaCAC1, gammaCAC2, GATA-1, GATA-2, GATA-3, GATA- 4, GATA-5, GATA-6, Gbx-1, Gbx-2, GCF, GCMa, GCNS, GF1, GLI, GLI1, GLI3, GR alpha, GR beta, GRF-1, Gsc, Gsc1, GT-IC, GT-IIA, GT-IIBalpha, GT-IIBbeta, H1TF1, H1TF2, H2RIIBP, H4TF-1, H4TF-2, HAND1, HAND2, HB9, HDAC1, HDAC2, HDAC3, hDaxx, heat-induced factor, HEB, HEB1-p67, HEB1-p94, HEF-1 B, HEF-1T, HEF-4C, HEN1, HEN2, Hesx1, Hex, HIF-1, HIF-1alpha, HIF-1beta, HiNF-A, HiNF-B, HINF-C, HINF-D, HiNF-D3, HiNF-E, HiNF-P, HIP1, HIV-EP2, Hlf, HLTF, HLTF (Met123), HLX, HMBP, HMG I, HMG I(Y), HMG Y, HMGI-C, HNF-1A, HNF-1B, HNF-1C, HNF-3, HNF-3alpha, HNF-3beta, HNF-3gamma, HNF4, HNF-4alpha, HNF4alpha1, HNF-4alpha2, HNF-4alpha3, HNF- 4alpha4, HNF4gamma, HNF-6alpha, hnRNP K, HOX11, HOXA1, HOXA10, HOXA10 PL2, HOXA11, HOXA13, HOXA2, HOXA3, HOXA4, HOXA5, HOXA6, HOXA7, HOXA9A, HOXA9B, HOXB-1, HOXB13, HOXB2, HOXB3, HOXB4, HOXB5, HOXB6, HOXA5, HOXB7, HOXB8, HOXB9, HOXC10, HOXC11, HOXC12, HOXC13, HOXC4, HOXC5, HOXC6, HOXC8, HOXC9, HOXD10, HOXD11, HOXD12, HOXD13, HOXD3, HOXD4, HOXD8, HOXD9, Hp55, Hp65, HPX42B, HrpF, HSF, HSF1 (long), HSF1 (short), HSF2, hsp56, Hsp90, IBP-1, ICER-II, ICER-ligamma, ICSBP, Id1, Id1 H′, Id2, Id3, Id3/Heir-1, IF1, IgPE-1, IgPE-2, IgPE-3, IkappaB, IkappaB-alpha, IkappaB-beta, IkappaBR, II-1 RF, IL-6 RE- BP, 11-6 RF, INSAF, IPF1, IRF-1, IRF-2, irlB, IRX2a, Irx-3, Irx-4, ISGF-1, ISGF-3, ISGF3alpha, ISGF-3gamma, 1st-1, ITF, ITF-1, ITF-2, JRF, Jun, JunB, JunD, kappay factor, KBP-1, KER1, KER-1, Kox1, KRF-1, Ku autoantigen, KUP, LBP-1, LBP-1a, LBX1, LCR- F1, LEF-1, LEF-1B, LF-A1, LHX1, LHX2, LHX3a, LHX3b, LHXS, LHX6.1a, LHX6.1b, LIT-1, Lmo1, Lmo2, LMX1A, LMX1B, L-My1 (long form), L-My1 (short form), L-My2, LSF, LXRalpha, LyF-1, LyI-1, M factor, Mad1, MASH-1, Max1, Max2, MAZ, MAZ1, MB67, MBF1, MBF2, MBF3, MBP-1 (1), MBP-1 (2), MBP-2, MDBP, MEF-2, MEF-2B, MEF-2C (433 AA form), MEF-2C (465 AA form), MEF-2C (473 M form), MEF-2C/delta32 (441 AA form), MEF-2D00, MEF-2D0B, MEF-2DA0, MEF-2DA′0, MEF-2DAB, MEF-2DA′B, Meis- 1, Meis-2a, Meis-2b, Meis-2c, Meis-2d, Meis-2e, Meis3, Meox1, Meox1a, Meox2, MHox (K- 2), Mi, MIF-1, Miz-1, MM-1, MOP3, MR, Msx-1, Msx-2, MTB-Zf, MTF-1, mtTF1, Mxi1, Myb, Myc (cMyc), Myc 1, Myf-3, Myf-4, Myf-5, Myf-6, MyoD, MZF-1, NC1, NC2, NCX, NELF, NER1, Net, NF III-a, NF NF NF-1, NF-1A, NF-1B, NF-1X, NF-4FA, NF-4FB, NF- 4FC, NF-A, NF-AB, NFAT-1, NF-AT3, NF-Atc, NF-Atp, NF-Atx, NfbetaA, NF-CLE0a, NF- CLE0b, NFdeltaE3A, NFdeltaE3B, NFdeltaE3C, NFdeltaE4A, NFdeltaE4B, NFdeltaE4C, Nfe, NF-E, NF-E2, NF-E2 p45, NF-E3, NFE-6, NF-Gma, NF-GMb, NF-IL-2A, NF-IL-2B, NF-jun, NF-kappaB, NF-kappaB(-like), NF-kappaB1, NF-kappaB1, precursor, NF-kappaB2, NF-kappaB2 (p49), NF-kappaB2 precursor, NF-kappaE1, NF-kappaE2, NF-kappaE3, NF- MHCIIA, NF-MHCIIB, NF-muE1, NF-muE2, NF-muE3, NF-S, NF-X, NF-X1, NF-X2, NF- X3, NF-Xc, NF-YA, NF-Zc, NF-Zz, NHP-1, NHP-2, NHP3, NHP4, NKX2-5, NKX2B, NKX2C, NKX2G, NKX3A, NKX3A v1, NKX3A v2, NKX3A v3, NKX3A v4, NKX3B, NKX6A, Nmi, N-Myc, N-Oct-2alpha, N-Oct-2beta, N-Oct-3, N-Oct-4, N-Oct-5a, N-Oct-5b, NP-TCII, NR2E3, NR4A2, Nrf1, Nrf-1, Nrf2, NRF-2beta1, NRF-2gamma1, NRL, NRSF form 1, NRSF form 2, NTF, O2, OCA-B, Oct-1, Oct-2, Oct-2.1, Oct-2B, Oct-2C, Oct-4A, Oct4B, Oct-5, Oct-6, Octa-factor, octamer-binding factor, oct-B2, oct-B3, Otx1, Otx2, OZF, p107, p130, p28 modulator, p300, p38erg, p45, p49erg,-p53, p55, p55erg, p65delta, p67, Pax-1, Pax- 2, Pax-3, Pax-3A, Pax-3B, Pax-4, Pax-5, Pax-6, Pax-6/Pd-5a, Pax-7, Pax-8, Pax-8a, Pax-8b, Pax-8c, Pax-8d, Pax-8e, Pax-8f, Pax-9, Pbx-1a, Pbx-1b, Pbx-2, Pbx-3a, Pbx-3b, PC2, PC4, PC5, PEA3, PEBP2alpha, PEBP2beta, Pit-1, PITX1, PITX2, PITX3, PKNOX1, PLZF, PO-B, Pontin52, PPARα, PPARβ, PPARgamma1, PPARγ2, PPUR, PR, PR A, pRb, PRD1-BF1, PRDI-BFc, Prop-1, PSE1, P-TEFb, PTF, PTFα, PTFβ, PTFdelta, PTFγ, Pu box binding factor, Pu box binding factor (BJA-B), PU.1, PuF, Pur factor, R1, R2, RAR-alpha1, RAR-β, RAR-β2, RAR-γ, RAR-γ1, RBP60, RBP-Jκ, Rel, RelA, RelB, RFX, RFX1, RFX2, RFX3, RFXS, RF- Y, RORα1, RORα2, RORα3, RORbeta, RORgamma, Rox, RPF1, RPGα, RREB-1, RSRFC4, RSRFC9, RVF, RXR-α, RXR-β, SAP-1a, SAP1b, SF-1, SHOX2a, SHOX2b, SHOXa, SHOXb, SHP, Sill-p110, SIII-p15, SIII-p18, SIM′, Six-1, Six-2, Six-3, Six-4, Six-5, Six-6, SMAD-1, SMAD-2, SMAD-3, SMAD-4, SMAD-5, SOX-11, SOX-12, Sox-4, Sox-5, SOX-9, Sp1, Sp2, Sp3, Sp4, Sph factor, Spi-B, SPIN, SRCAP, SREBP-1a, SREBP-1b, SREBP-1c, SREBP-2, SRE-ZBP, SRF, SRY, SRP1, Staf-50, STAT1alpha, STAT1beta, STAT2, STAT3, STAT4, STATE, T3R, T3R-α1, T3R-α2, T3R-beta, TAF(I)110, TAF(I)48, TAF(I)63, TAF(II)100, TAF(II)125, TAF(II)135, TAF(II)170, TAF(II)18, TAF(II)20, TAF(II)250, TAF(II)250Delta, TAF(II)28, TAF(II)30, TAF(II)31, TAF(II)55, TAF(II)70-α, TAF(II)70-β, TAF(II)70-γ, TAF-I, TAF-II, TAF-L, Tal-1, Tal-1beta, Tal-2, TAR factor, TBP, TBX1A, TBX1B, TBX2, TBX4, TBXS (long isoform), TBXS (short isoform), TCF, TCF-1, TCF-1A, TCF-1B, TCF-1C, TCF-1D, TCF-1E, TCF-1F, TCF-1G, TCF-2alpha, TCF-3, TCF-4, TCF- 4(K), TCF-4B, TCF-4E, TCFbeta1, TEF-1, TEF-2, tel, TFE3, TFEB, TFIIA, TFIIA-α/β precursor, TFIIA-alpha/beta precursor, TFIIA-gamma, TFIIB, TFIID, TFIIE, TFIIE-α, TFIIE- β, TFIIF, TFIIF-α, TFIIF-β, TFIIH, TFIIH*, TFIIH-CAK, TFIIH-cyclin H, TFIIH- ERCC2/CAK, TFIIH-MAT1, TFIIH-MO15, TFIIH-p34, TFIIH-p44, TFIIH-p62, TFIIH-p80, TFIIH-p90, TFII-I, Tf-LF1, Tf-LF2, TGIF, TGIF2, TGT3, THRA1, TIF2, TLE1, TLX3, TMF, TR2, TR2-11, TR2-9, TR3, TR4, TRAP, TREB-1, TREB-2, TREB-3, TREF1, TREF2, TRF (2), TTF-1, TXRE BP, TxREF, UBF, UBP-1, UEF-1, UEF-2, UEF-3, UEF-4, USF1, USF2, USF2b, Vav, Vax-2, VDR, vHNF-1A, vHNF-1B, vHNF-1C, VITF, WSTF, WT1, WT1I, WT1 I-KTS, WT1 I-del2, WT1-KTS, WT1-del2, X2BP, XBP-1, XW-V, XX, YAF2, YB-1, YEBP, YY1, ZEB, ZF1, ZF2, ZFX, ZHX1, ZIC2, ZID, ZNF174, amongst others. It is contemplated that the transcription factor can be an E-box transcription factor capable of binding an E-box transcription factor binding site or domain (i.e., an enhancer box or E-box). Generally, an E-box is a DNA response element found in some eukaryotes that acts as a protein binding site and has been shown to regulate gene expression in a range of cells and tissues. Accordingly, the binding site of the hairpin oligonucleotide may comprise, consist of or consist essentially of an E-box binding site, as are known in the art. Suitably, such binding sites comprise, consist of or consist essentially of a nucleotide sequence of 5'-CANNTG-3' (SEQ ID NO: 4; i.e., a consensus E-box binding site sequence), wherein N can be any nucleotide (e.g., A, C, T, G or U). In certain examples, the E-box binding site comprises, consists of or consists essentially of a nucleotide sequence of 5'-CAC[GA]TG-3' (SEQ ID NO: 5) (wherein [GA] or [G/A] indicates a nucleotide variation of G or A at this position) or more particularly 5'- CACGTG-3' (SEQ ID NO: 6) or 5'-CACATG-3' (SEQ ID NO: 7), or a nucleotide sequence having one or two substitutions, deletions, or insertions therein. The substitutions, deletions, or insertions may be any substitution, deletion, or insertion of a single nucleotide such that the E- box transcription factor binding site retains at least one of its endogenous functions (e.g., an ability to bind an E-box transcription factor). By way of example, one or more of the thymine residues may be replaced or substituted by uracil residues or vice versa (e.g., 5'-CANNUG-3' (SEQ ID NO: 14), 5'-CAC[GA]UG-3' (SEQ ID NO: 11), 5'-CACGUG-3' (SEQ ID NO: 12) or 5'-CACAUG-3' (SEQ ID NO: 13)). In addition to the above, non-canonical E-boxes are also known in the art. As such, in alternative examples, the E-box binding site comprises, consists of, consists essentially of a nucleotide sequence of 5'- CACGTT-3' (SEQ ID NO: 8), 5'- CAGCTT-3' (SEQ ID NO: 9) or 5'-CACCTCGTGAC-3' (SEQ ID NO: 10), or a nucleotide sequence having one or two substitutions, deletions, or insertions therein. For such examples and when incorporated into a hairpin oligonucleotide, one or more of the thymine residues may be replaced or substituted by uracil residues or vice versa (e.g., 5'- CACGUU-3' (SEQ ID NO: 15), 5'- CACGUT-3' (SEQ ID NO: 16), 5'- CACGTU-3' (SEQ ID NO: 17), 5'- CAGCUU-3' (SEQ ID NO: 18), 5'- CAGCUT-3' (SEQ ID NO: 19), 5'- CAGCTU-3' (SEQ ID NO: 20), 5'-CACCUCGUGAC-3' (SEQ ID NO: 21), 5'-CACCTCGUGAC-3' (SEQ ID NO: 22) or 5'-CACCUCGTGAC-3' (SEQ ID NO: 23)). Exemplary E-box transcription factors include Myc/Max, Fos/Jun, HIF1α/β, MITF, MyoD, HES family, Hey family, ID1/2/3, E2 family, Twist, AHR, AHRR, ARNT, ARNT2, ARNTL, ARNTL2, ASCL1, ASCL2, ASCL3, ASCL4, ATF1, ATF2, ATF4, ATF5, ATF6, ATF7, ATOH1, ATOH7, ATOH8, BACH1, BACH2, BATF, BATF2, BHLHB2, BHLHB3, BHLHB4, BHLHB5, BHLHB8, CLOCK, CREB1, CREB3, CREB3L1, CREB3L2, CREB3L3, CREB3L4, CREB5, CREBL1, CREM, E4BP4, EPAS1, FERD3L, FIGLA, FOSL1, FOSL2, HAND1, HAND2, HES1, HES2, HES3, HES4, HES5, HES6, HES7, HEY1, HEY2, HIF1A, ID1, ID2, ID3, ID4, JUN, JUNB, JUND, KIAA2018, LYL1, MASH1, MATH2, MAX, MESP1, MESP2, MIST1, MITF, MLX, MLXIP, MLXIPL, MNT, MSC, MSGN1, MXD1, MXD3, MXD4, MXI1, MYC, MYCL1, MYCL2, MYCN, MYF5, MYF6, MYOD1, MYOG, NCOA1, NCOA3, NEUROD1, NEUROD2, NEUROD4, NEUROD6, NEUROG1, NEUROG2, NEUROG3, NFE2, NFE2L2, NFE2L3, NHLH1, NHLH2, NPAS1, NPAS2, NPAS3, OAF1, OLIG1, OLIG2, OLIG3, OPAQUE2, PTF1A, SCL, SCXB, SIM1, SIM2, SNFT, SOHLH1, SOHLH2, SREBF1, SREBF2, TAL1, TAL2, TCF12, TCF15, TCF21, TCF3, TCF4, TCFL5, TFAP4, TFE3, TFEB, TFEC, TWIST1, TWIST2, USF1 and USF2. In particular examples, the target protein is cMyc (inclusive of the cMyc-Max protein complex). cMyc is a protooncogene, which is overexpressed in a wide range of human cancers. When it is specifically mutated, or overexpressed, it increases cell proliferation and functions as an oncogene. The MYC gene encodes for a transcription factor that regulates expression of 15% of all genes through binding on Enhancer Box sequences (E-boxes) and recruiting histone acetyltransferases (HATs). cMyc belongs to the Myc family of transcription factors, which also includes nMyc and lMyc. Myc-family transcription factors contain the bHLH/LZ (basic Helix- Loop-Helix Leucine Zipper) domain. In some examples, cMyc protein or simply cMyc relates to human cMyc. A non-limiting example of a cMyc amino acid sequence from humans may be found under accession number P01106 (UniProtKB). An exemplary amino acid sequence for a full length cMyc is provided in SEQ ID NO: 2 below: cMyc protein (SEQ ID NO:2) MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPP LSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPD DETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQD LSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVL HEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRC HVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHN VLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLL RKRREQLKHKLEQLRNSCA cMyc is known to bind DNA in a non-specific manner, but can also specifically recognize the core sequence of 5'-CAC[GA]TG-3' (SEQ ID NO: 5). Accordingly, the binding site of the hairpin oligonucleotide may comprise, consist of or consist essentially of the nucleic acid sequence of 5'-CAC[GA]TG-3' (SEQ ID NO: 5) or 5'-CAC[GA]UG-3' (SEQ ID NO: 11). Referring to some examples, the binding site of the hairpin oligonucleotide comprises, consists of or consists essentially of a nucleic acid sequence of 5'-CACGTG-3' (SEQ ID NO: 6), 5'- CACGUG-3' (SEQ ID NO: 12), 5'-CACATG-3' (SEQ ID NO: 7), 5'-CACAUG-3' (SEQ ID NO: 13) or a fragment, variant or derivative thereof. In particular examples, the binding site of the hairpin oligonucleotide comprises, consists of or consists essentially of the nucleic acid sequence of 5'-CACGTG-3' (SEQ ID NO: 6) or 5'-CACGUG-3' (SEQ ID NO: 12). In other examples, the binding site of the hairpin oligonucleotide comprises, consists of or consists essentially of the nucleic acid sequence of 5'-CACATG-3' (SEQ ID NO: 7) or 5'-CACAUG-3' (SEQ ID NO: 13). Suitably, the binding site of the hairpin oligonucleotide comprises, consists of or consists essentially of the nucleic acid sequence of 5'-GAGCAC[GA]UGGUU-3' (SEQ ID NO: 31), wherein one or more of the U nucleotides may be a T. In some examples, the binding site of the hairpin oligonucleotide comprises, consists of or consists essentially of the nucleic acid sequence of 5'-GAGCACGUGGUU-3' (SEQ ID NO: 3) or a fragment, variant or derivative thereof. Such variants may include the nucleotide sequence of 5'-GAGCACAUGGUU-3' (SEQ ID NO: 32), wherein one or more of the U nucleotides may be a T. The nucleotide sequence of SEQ ID NO: 3 represents the NPM1 gene’s E-box promoter sequence inclusive of adjacent, flanking or surrounding base pairs, which is regarded as a high affinity binding site for cMyc. With respect to the binding site of SEQ ID NO:3, it is envisaged that one or more of the U nucleotides may be a T (e.g., 5'-GAGCACGTGGUU-3' (SEQ ID NO: 24), 5'- GAGCACGTGGTU-3' (SEQ ID NO: 25), 5'-GAGCACGTGGTT-3' (SEQ ID NO: 26), 5'- GAGCACGTGGUT-3' (SEQ ID NO: 27), 5'-GAGCACGUGGTU-3' (SEQ ID NO: 28), 5'- GAGCACGUGGUT-3' (SEQ ID NO: 29) or 5'-GAGCACGUGGTT-3' (SEQ ID NO: 30)). Suitably, the hairpin oligonucleotide, in a single stranded form, comprises, consists of or consists essentially of the nucleic acid sequence of 5'- GAGCACGUGGUUAAAAAACCACGUGCUC-3' (SEQ ID NO: 1; Figure 1) or a fragment, variant or derivative thereof. Again, it will be understood that one or more of the U nucleotides of SEQ ID NO: 1 may be a T. It is contemplated that one or more of the nucleotides and/or the internucleotide linkages of SEQ ID NO: 1 can be modified, such as described herein. In particular examples, all of the internucleotide linkages of SEQ ID NO: 1 comprise a phosphorothioate modification. In certain examples, the 3’ terminal cytosine (C) residue of SEQ ID NO: 1 comprises a 2’OMe modification. In other examples, the 5’ terminal guanine (G) residue of SEQ ID NO: 1 comprises a 2’OMe modification. According to other examples, the 3’ terminal cytosine (C) residue and the 5’ terminal guanine (G) residue of SEQ ID NO: 1 comprises a 2’OMe modification. For particular examples, all of the internucleotide linkages of SEQ ID NO: 1 comprise a phosphorothioate modification and all of the nucleic acid bases of SEQ ID NO: 1 are modified, such as by way of a 2’OMe modification (e.g., 5′- mG*mA*mG*mC*mA*mC*mG*mU*mG*mG*mU*mU*mA*mA*mA*mA*mA*mA*mC *mC*mA*mC*mG*mU*mG*mC*mU*mC-3′; phosphorothioate modified internucleotide linkages are indicated by and 2′-OMe modified nucleic acid bases are indicated by “m”). It is known that cMyc may function in conjunction with Max. These two transcription factors can form a heterodimer on the promoter of a target gene. There are low and high affinity targets for cMyc:Max and thus cMyc’s expression is typically fine-tuned to only drive activation of specific promoters in the context of cell type. In view of the above, the hairpin oligonucleotide can inhibit Myc/Max activity or function, such as by interfering with Myc/Max binding to DNA (e.g., a E-box transcription factor binding site or another DNA binding site, such as those described herein). As used herein, the phrase “inhibits Myc/Max activity” or variations thereof means that after administration of an hairpin oligonucleotide described herein, such as that of SEQ ID NO: 1, to an animal or a cell, an activity of Myc/Max in the animal or cell, such as the ability of this protein complex to bind E boxes, is abrogated or reduced. In various examples, the activity of Myc/Max is less than about 95%, 90%, 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10%, 5%, 2% or 1% of the activity in the absence of the hairpin oligonucleotide. Formulation In a particular form, the pharmaceutical compositions described herein comprise an acceptable carrier, diluent or excipient. By “acceptable carrier, diluent or excipient” is meant a solid or liquid filler, diluent or encapsulating substance that may be safely used in systemic administration. Depending upon the particular route of administration, a variety of carriers, diluent and excipients well known in the art may be used. These may be selected from a group including sugars, starches, cellulose and its derivatives, malt, gelatine, talc, calcium sulfate, vegetable oils, synthetic oils, polyols, alginic acid, phosphate buffered solutions, emulsifiers, isotonic saline and salts such as mineral acid salts including hydrochlorides, bromides and sulfates, organic acids such as acetates, propionates and malonates, water and pyrogen-free water. A useful reference describing acceptable carriers, diluents and excipients is Remington’s Pharmaceutical Sciences (Mack Publishing Co. N.J. USA, 1991) which is incorporated herein by reference. Hairpin oligonucleotides of the disclosure may be admixed, encapsulated, conjugated (such as fused) or otherwise associated with other molecules, molecule structures or mixtures of compounds, resulting in, for example, liposomes, receptor-targeted molecules, oral, rectal, topical or other formulations, for assisting in uptake, distribution and/or absorption. Representative United States patents that teach the preparation of such uptake, distribution and/or absorption-assisting formulations include, but are not limited to, US 5,108,921, US 5,354,844, US 5,416,016, US 5,459,127, US 5,521,291, US 5,543,158, US 5,547,932, US 5,583,020, US 5,591,721, US 4,426,330, US 4,534,899, US 5,013,556, US 5,108,921, US 5,213,804, US 5,227,170, US 5,264,221, US 5,356,633, US 5,395,619, US 5,416,016, US 5,417,978, US 5,462,854, US 5,469,854, US 5,512,295, US 5,527,528, US 5,534,259, US 5,543,152, US 5,556,948, US 5,580,575, and US 5,595,756. The hairpin oligonucleotides may be formulated as pharmaceutically acceptable salts, esters, or salts of the esters, or any other compounds which, upon administration are capable of providing (directly or indirectly) the biologically active metabolite. The term “pharmaceutically acceptable salts” as used herein refers to physiologically and pharmaceutically acceptable salts of the oligonucleotide that retain the desired biological activities of the parent compounds and do not impart undesired toxicological effects upon administration. Examples of pharmaceutically acceptable salts and their uses are further described in US 6,287,860. It is further envisaged that the hairpin oligonucleotides provided herein may be prodrugs or pharmaceutically acceptable salts of the prodrugs, or other bioequivalents. The term “prodrugs” as used herein refers to therapeutic agents that are prepared in an inactive form that is converted to an active form (i.e., a drug) upon administration by the action of endogenous enzymes or other chemicals and/or conditions. In particular, prodrug forms of the oligonucleotide of the disclosure are prepared as SATE [(S acetyl-2-thioethyl) phosphate] derivatives according to the methods disclosed in WO 93/24510, WO 94/26764 and US 5,770,713. A prodrug may, for example, be converted within the body, such as by hydrolysis in the blood, into its active form that has medical effects. Pharmaceutical acceptable prodrugs are described in T. Higuchi and V. Stella, Prodrugs as Novel Delivery Systems, Vol. 14 of the A. C. S. Symposium Series (1976); "Design of Prodrugs" ed. H. Bundgaard, Elsevier, 1985; and in Edward B. Roche, ed., Bioreversible Carriers in Drug Design, American Pharmaceutical Association and Pergamon Press, 1987. Those skilled in the art of organic chemistry will appreciate that many organic compounds can form complexes with solvents in which they are reacted or from which they are precipitated or crystallized. These complexes are known as "solvates". For example, a complex with water is known as a "hydrate". In some examples, the hairpin oligonucleotides of the present disclosure can be complexed with a complexing agent to increase cellular uptake thereof. An example of a complexing agent includes cationic lipids. Cationic lipids can be used to deliver oligonucleotides to cells. The term “cationic lipid” includes lipids and synthetic lipids having both polar and non-polar domains and which are capable of being positively charged at or around physiological pH and which bind to polyanions, such as nucleic acids, and facilitate the delivery of nucleic acids into cells. In general, cationic lipids include saturated and unsaturated alkyl and alicyclic ethers and esters of amines, amides, or derivatives thereof. Straight-chain and branched alkyl and alkenyl groups of cationic lipids can contain, e.g., from 1 to about 25 carbon atoms. Exemplary straight chain or branched alkyl or alkene groups have six or more carbon atoms. Alicyclic groups include cholesterol and other steroid groups. Cationic lipids can be prepared with a variety of counterions (anions) including, e.g., Cl-, Br-, I-, F-, acetate, trifluoroacetate, sulfate, nitrite, and nitrate. Examples of cationic lipids include polyethylenimine, polyamidoamine (PAMAM) starburst dendrimers, Lipofectin (a combination of DOTMA and DOPE), Lipofectase, LIPOFECTAMINE ^TM (e.g., LIPOFECTAMINE ^TM 2000), DOPE, Cytofectin (Gilead Sciences, Foster City, Calif.), and Eufectins (JBL, San Luis Obispo, Calif.). Exemplary cationic liposomes can be made from N-[1-(2,3-dioleoloxy)-propyl]-N,N,N-trimethylammonium chloride (DOTMA), N-[1-(2,3-dioleoloxy)-propyl]-N,N,N-trimethylammonium methylsulfate (DOTAP), 3.beta.-[N--(N',N'-dimethylaminoethane)carbamoyl]cholesterol (DC-Chol), 2,3,- dioleyloxy-N-[2(sperminecarboxamido)ethyl]-N,N-dimethyl-1-pr opanaminium trifluoroacetate (DOSPA), 1,2-dimyristyloxypropyl-3-dimethyl-hydroxyethyl ammonium bromide; and dimethyldioctadecylammonium bromide (DDAB). Oligonucleotides can also be complexed with, e.g., poly (L-lysine) or avidin and lipids may, or may not, be included in this mixture, e.g., steryl-poly (L-lysine). Cationic lipids have been used in the art to deliver oligonucleotides to cells (see, e.g., US 5,855,910; 5,851,548; 5,830,430; 5,780,053; 5,767,099; Lewis et al., 1996; Hope et al., 1998). In addition to those listed above, other lipid compositions are also known in the art and include, for example, those taught in US 4,235,871; US 4,501,728; 4,837,028; 4,737,323. In some examples, lipid compositions can further comprise agents (e.g., viral proteins) to enhance lipid-mediated transfections of oligonucleotides. In further examples, N-substituted glycine oligonucleotides (peptoids) can be used to optimize uptake of oligonucleotides into tissues and cells. In various examples, a composition for delivering hairpin oligonucleotides of the present disclosure comprises a peptide having from between about one to about four basic residues. These basic residues can be located, e.g., on the amino terminal, C-terminal, or internal region of the peptide. Families of amino acid residues having similar side chains have been defined in the art. These families include amino acids with basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., glycine (can also be considered non-polar), asparagine, glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine). Apart from the basic amino acids, a majority or all of the other residues of the peptide can be selected from the non-basic amino acids, e.g., amino acids other than lysine, arginine, or histidine. Suitably, a preponderance of neutral amino acids with long neutral side chains are used. Suitably, the hairpin oligonucleotides are modified by attaching a peptide sequence that transports the oligonucleotide into a cell, referred to herein as a “transporting peptide”. In one example, the composition includes an oligonucleotide and a covalently attached transporting peptide. In further examples, the hairpin oligonucleotide is attached to a targeting moiety such as N- acetylgalactosamine (GalNAc), an antibody, an antibody-like molecule or aptamer (see, for example, Toloue and Ford (2011) and Esposito et al. (2018)). Administration Any safe route of administration may be employed, including oral, rectal, parenteral, sublingual, buccal, intravenous, intra-articular, intra-muscular, intra-dermal, subcutaneous, inhalational, intranasal, intraocular, intraperitoneal, intracerebroventricular, topical, mucosal and transdermal administration, although without limitation thereto. In one example, the oligonucleotide of the disclosure is administered systemically. As used herein “systemic administration” is a route of administration that is either enteral or parenteral. Dosage forms include tablets, dispersions, suspensions, injections, solutions, syrups, troches, capsules, nasal sprays, suppositories, aerosols, transdermal patches and the like. These dosage forms may also include injecting or implanting controlled releasing devices designed specifically for this purpose or other forms of implants modified to act additionally in this fashion. Controlled release may be effected by coating with hydrophobic polymers including acrylic resins, waxes, higher aliphatic alcohols, polylactic and polyglycolic acids and certain cellulose derivatives such as hydroxypropylmethyl cellulose. In addition, the controlled release may be effected by using other polymer matrices, liposomes and/or microspheres. Compositions may be presented as discrete units such as capsules, sachets, functional foods/feeds or tablets each containing a pre-determined amount of one or more therapeutic agents of the disclosure, as a powder or granules or as a solution or a suspension in an aqueous liquid, a non-aqueous liquid, an oil-in-water emulsion or a water-in-oil liquid emulsion. Such compositions may be prepared by any of the methods of pharmacy but all methods include the step of bringing into association one or more agents as described above with the carrier which constitutes one or more necessary ingredients. In general, the compositions are prepared by uniformly and intimately admixing the agents of the disclosure with liquid carriers or finely divided solid carriers or both, and then, if necessary, shaping the product into the desired presentation. The above compositions may be administered in a manner compatible with the dosage formulation, and in such amount as effective. The dose administered to a subject, in the context of the present disclosure, should be sufficient to effect a beneficial response in a subject over an appropriate period of time. The quantity of agent(s) to be administered may depend on the subject to be treated inclusive of the age, sex, weight and general health condition thereof, factors that will depend on the judgement of the practitioner. Design and Testing of Candidate Oligonucleotides In another form, the present disclosure provides a method for selecting a hairpin oligonucleotide for inhibiting a target protein, said method including the steps of: (a) producing one or more candidate hairpin oligonucleotides comprising a loop region and a double-stranded linear region, wherein the double-stranded linear region comprises a binding or recognition site for the target protein; (b) testing the ability of the one or more candidate hairpin oligonucleotides to bind and/or inhibit the target protein, and (c) selecting a hairpin oligonucleotide which binds and/or inhibits the target protein. Suitably, the hairpin oligonucleotide, inclusive of modifications thereof, and the target protein are that hereinbefore described. In addition to design elements of the present disclosure, there are many known factors to be considered when producing a hairpin oligonucleotide. The specifics depend on the purpose of the oligonucleotide but include features such as strength and stability of the oligonucleotide- target protein interaction, such as the secondary structure of the hairpin oligonucleotide, thermodynamic stability, the position of the DNA-binding domain of the target protein, and/or functional motifs. As used herein, the phrase “inhibits the target protein” or “inhibits an activity of the target protein” or variations thereof means that after administration of a hairpin oligonucleotide to an animal or cell, the animal or cell is not able to elicit a target protein-based biological or cellular response or is only able to elicit a reduced or partial target protein-based biological or cellular response, such as those biological or cellular responses that are dependent upon the target protein binding to endogenous nucleic acid, when compared to a control or reference sample (e.g., control cells not treated with the candidate oligonucleotide). As such, the present method may include a further step that measures or detects a change in one or more biological activities of the target protein in a cell or an animal in response to the candidate oligonucleotide(s). In some examples, the activity of the target protein is less than about 95%, 90%, 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10%, 5%, 2% or 1% of the activity in the absence of the candidate oligonucleotide (e.g., untreated control cells). Accordingly, the level of activity of a target protein may also be compared to a reference or threshold level thereof. Thus, any of the methods disclosed herein may comprise a step of establishing a reference or threshold level activity of the target protein. Once synthesized, candidate hairpin oligonucleotides can be tested for their desired activity using standard procedures in the art. This may involve administering the candidate to cells in vitro expressing the target protein and measuring binding and/or inhibition thereof by the candidate hairpin oligonucleotide (e.g., analysing the amount of transcription of a target gene of the target protein, such as RNA and/or protein) and/or utilising one or more functional assays (e.g., cell growth and proliferation, apoptosis, cellular differentiation) to determine whether the activity thereof changes after exposure to a candidate hairpin oligonucleotide. In another example, the candidate oligonucleotide is administered to an animal, and the animal screened for the amount of target protein inhibition. In other examples, the candidate hairpin oligonucleotide is tested for its ability to bind or hybridize to a target protein, such as by those methods described herein (e.g., assess affinity by EMSA assay). In some examples, inhibitory activity of the candidate hairpin oligonucleotides, and more particularly those containing a binding site for a transcription factor, can be assessed by mRNA reverse transcription quantitative real-time PCR (RT-qPCR) to determine expression of a target gene. For example, RNA can be extracted and purified from cells which have been incubated with a candidate oligonucleotide. cDNA is then synthesized from isolated RNA and RT-qPCR can be performed, using methods and reagents known the art. Protein products and/or downstream cell signalling (and/or one or more markers thereof) of a target gene may alternatively or additionally be determined, such as by any means known in the art, including, but not limited to, ELISA, western blot, mass spectrometry, proteomics, immunoprecipitation and immunostaining. Suitably, the candidate hairpin oligonucleotide possesses or displays little or no significant off- target and/or nonspecific effects. It is also contemplated that the candidate hairpin oligonucleotide may be rationally designed or engineered de novo based on desired or predicted structural characteristics or features that indicate the candidate oligonucleotide could bind and/or block or inhibit one or more biological activities of the target protein. An initial step of the method may include identifying a plurality of candidate oligonucleotides that are selected according to broad structural and/or functional attributes, such as an ability to bind or specifically bind the target protein. Additionally, the present method may further include one or more of the steps of: selecting the candidate hairpin oligonucleotide that binds (e.g., specifically binds with high affinity) and/or modulates the expression and/or the activity of the target protein; isolating or purifying the candidate hairpin oligonucleotide; formulating the candidate hairpin oligonucleotide into a pharmaceutical formulation; and adding the candidate hairpin oligonucleotide or the pharmaceutical formulation to packaging and/or a container. Accordingly, in another form, the present disclosure provides a hairpin oligonucleotide designed, selected or identified by the present methods. So that preferred embodiments of the present disclosure may be fully understood and put into practical effect, reference is made to the following non-limiting examples. Examples Example 1. This Example tested the ability of the DRpinMyc hairpin oligonucleotide to bind and functionally inhibit the cMyc/Max protein complex. The Drpin oligonucleotide design described herein differs from antisense oligonucleotides as it is designed to bind proteins and not DNA or RNA. Drpin is a single stranded, self folding, synthetic RNA oligonucleotide, as described in more detail above. The oligonucleotide folds into a hairpin, which usually has a fully Watson and Crick base pairing stem or contains nucleotides that will induce a specific secondary structure, which will be recognised by a target protein (see Figure 1). cMyc was chosen as the target protein to validate this technology with. The Myc family in humans is composed c-myc (MYC), l-myc (MYCL), and n-myc (MYCN). C-MYC is the best characterised as it is involved in up to 70% of human cancers. N-MYC has been shown to be involved in brain cancer, prostate cancers and well a blood cancers. While MYC is one of the common oncogenes driving cancer it has been difficult to target due to is lack of a stable structure. Materials & Methods EMSA assay To confirm the interaction between Drpin and c-Myc and the cMyc:Max heterodimer, electromobility shift assays (EMSA) were performed using the Drpin compound. The oligomeric compounds were labelled with FAM or Cy5, incubated with varying amounts of c- Myc or c-Myc:Max, and bound and free oligomers were separated by native gel electrophoresis. Notably, both c-Myc and c-Myc:Max retarded the migration of the tumour- modulating Drpin with significantly higher affinity than cMyc bound to the same sequence as DNA. Purified cMyc and c-Myc:Max was incubated with 10 nM of labelled oligo for15 min at 37° C in a buffer consisting of 10 mM Tris-HCI (pH8.0), 100 mM NaCl, 0.01 % IGEPAL, 125 mM EDTA and 100 ng/μL BSA. Samples were separated by electrophoresis on a 10% PAGE gel in TBE buffer for 60 min at 80V at 4° C. Molecular dynamics and in silico modelling Drpin Modelling The Drpin oligonucleotide secondary structure was predicted by MC-Fold, accessible as a web server at https://www.major.iric.ca/MC-Fold/. RNA tertiary structure models of Drpin were generated by providing the sequence and MC-Fold secondary structure to RNAcomposer at https://rnacomposer.cs.put.poznan.pl/. Conversion of the RNAComposer tertiary structure to the R _P and S _p Phosphorothioate with 2′-O-Methyl chemistry was performed with PyMOL from Schrödinger, Inc (Schrödinger, L. & DeLano, W., 2020. PyMOL, Available at: http://www.pymol.org/pymol.). Molecular Dynamics Setup and Simulation A novel force field library was required for the ribonucleotide chemistry used in Drpin. The library was created using the R.E.D. server at https://upjv.q4md-forcefieldtools.org/. The Drpin model was solvated in 0.15 M NaCl with TIP3P water molecules added to a padding distance of 15 Å in a truncated octahedron in tleap from the Ambertools16 suite. Atomistic Molecular Dynamics simulations were performed at 300 K for 1 μs for RNA and both stereoisomers of Drpin using pmemd.cuda from the Amber 2020 package. Trajectory Analysis Cpptraj from AmberTools 16 was used to analyse simulation trajectories. K-means Clustering was calculated by sorting into two clusters based on intra-cluster RMSD measured via Davies- Bouldin Index and inter-cluster RMSD measured via pseudo-F. 3D structures of oligomers were processed, and figures were generated with ChimeraX from the University of California San Francisco. Western blotting Western/Immuno blots were performed as described previously (Bolderson et al., 2014, Nucleic Acids Res., 42, 6326–6336) and visualized using an Odyssey infrared imaging system. When necessary, immunoblots were quantified using ImageJ software and normalized to actin. Transfection of DrpinMyc Transfections of Drpin were performed using Lipofectamine RNAimax (Life Technologies) as per manufacturer’s instructions for siRNA transfection. Cell culture Cells were maintained in Roswell Park Memorial Institute medium (DMEM, Sigma). All cell culture media was supplemented with 10% fetal bovine serum (Sigma). Cells were grown in an atmosphere of 21% oxygen and 5% CO2 at 37◦C. Incucyte analysis A panel of breast cancer cell lines, including MCF7 (hormone positive) and MDA-MB-231 (triple-negative breast cancer) were evaluated to examine the impact of Drpin on cellular proliferation. All cell lines were maintained in DMEM medium supplemented with 10% FBS. All cell lines were cultured at 37°C in a humidified 5% CO ₂ atmosphere. Lipofectamine RNAimax (Life technologies) was used to aid Drpin delivery. For all cell lines, 2.5 x 10 ³ cells were seeded into clear walled 96-well plates and four regions per well were imaged every two hours over a period of 120 h using the Incucyte Zoom (Essen Biosciences). Image analysis was conducted using the Incucyte Zoom software package. Flow cytometry Cell pellets were created by spinning at 11,000rpm for 3min in eppendorf tubes and removing the supernatant. Pellets were resuspended in 180μl of 70% ethanol and stored at 4°C overnight. The cells were re-pelleted at 14,000g 1min, S/N removed and each sample resuspended in 200μl PI solution (2.2.1) with Rnase A added 1:100v/v (100μg/ml final). Analyse on FACS 2D histogram for PI. Results To determine if the Drpin could bind to cMyc and cMyc:Max, the inventors conducted a EMSA assay with increasing concentrations of Drpin. It was demonstrated that the Drpin binds to cMyc alone and the cMyc:Max dimer with an IC50 of 46 nM and 107 nM respectively (Figure 2). It has been established that the affinity of cMyc:Max for its substrates is typically in excess of 10uM. The inventors next used molecular dynamics and in silico modelling to determine the likely mode of Drpin binding to cMyc:Max. The proposed binding mechanism isillustrated in Figure 3. To explore this further, the inventors next sought to determine if DrpinMyc had an impact on cell growth in cMyc driven tumours. Depletion of cMyc by siRNA does not result in cell death, but does infer a blockade of the cell cycle, and can occur in G1, S or G2 phases of the cell cycle. Triple negative breast cancer is known to be primarily driven by cMyc. Previous studies have shown that triple negative breast cancer (TNBC) lines have the highest levels of cMyc (reference: (https://www.nature.com/articles/s41419-020-02980-2)). The inventors then sought to treat TNBC cell lines with DrpinMyc. To do this, DrpinMyc was transfected into cells at varying concentrations. As expected, the DrpinMyc oligonucleotide did not kill cells to any great degree over the time period of the experiment (Figure 4). It was confirmed that DrpinMyc was not inducing death under the time points of these experiments. However, it was noticed that treated cells did not appear to be dividing further. To explore this, the inventors next treated cells with DrpinMyc and examined cell doubling/growth using an IncuCyte Zoom® system (Figure 5). A number of concentrations of DrpinMyc were utilised so that an IC50 for growth inhibition could be calculated. The data in Figure 5 generally demonstrates that DrpinMyc causes a dose-dependent reduction in cell proliferation in each the TNBC cell lines. While a loss of growth or proliferation is indicative of cell cycle arrest, this can be confirmed by using flow cytometry using propidium iodide (PI) staining of the DNA. (Figure 6). This demonstrated that TNBC cells were indeed arresting and that cell cycle arrest could result in death over an extended period of time. This phenotype resembles that seen with cells subjected to inhibition of cMyc with siRNA or shRNA. Example 2 Example 1 confirmed that DrpinMyc was capable of arresting cancer cell line growth at a number of different stages of the cell cycle. However, this did not prove on-target activity for this oligonucleotide. To determine this in Example 2, the inventors treated MCF7 and MDA- MB-231 cells with DrpinMyc or with a negative RNA sequence of the same chemistry and investigated gene expression profiles of these respective treatment groups. Materials & methods Cell treatment MCF7 and MDA-MB-231breast cancer cell lines (“NEG”) were treated with vehicle (“MOCK”) or DrpinMyc (“DR”). Transcriptomic differential expression analysis was done for contrasts 231-DR_vs_231-NEG, 231-DR_vs_231-MOCK, MCF7-DR_vs_MCF7-NEG and MCF7-DR_vs_MCF7-MOCK. RNAseq Each dataset was processed individually for sequencing quality using FastQC. Upon passing quality criteria, reads were aligned against Human genome using STAR aligner. Subsequently, gene and transcript level abundance were estimated with RSEM tool, followed by differential expression analysis using DESeq2 R package. Gene level summarization counts were normalized to library size and batch-effects were corrected for unbiased comparison. Significant differentially expressing genes were identified with significance scores calculated and provided separately for further analysis. Raw data processing & read counting Prior to differential expression (DE) analysis, raw reads were evaluated for quality check in terms of sequencing quality, contamination and over-representation of sequences. Reads were then aligned to latest reference genome (GRCh38) with GTF from Gencode (v39) using STAR aligner (Dobin et al, 2013). Post alignment, efforts have been made to utilise the unmapped reads by trimming to dynamic minimum of 36bp length for realignment. Aligned reads were transformed into read counts per gene/transcript using RSEM tool (Li et al, 2011). Differential expression Pairwise differential expression analysis was performed using DESeq2 R package (Love et al, 2014) with Control/Untreated samples being reference for individual experiments. Briefly, expression counts were scaled and normalized to correct the sequencing depth and batch differences among samples. These normalized counts were then used for differential expression analysis and to generate fold change values in log2 scale for contrasts 231-DR_vs_231-NEG, 231-DR_vs_231-MOCK,MCF7-DR_vs_MCF7-NEGandMCF7-DR_vs_MCF7-MOC K [hereafter fold changes values refer to Log2FC = log2(sample/control)]. Genes with lower read count can generate higher fold change values, which may lead to possible false positives. Hence, to adjust the fold changes that arose due to ratio between lower read counts in samples, the inventors employed a fold change shrinkage estimator approach from DESeq2. Gene prioritization To highlight the statistically significant genes that were differentially expressed, the inventors selected the genes with fold change beyond +1 and adjusted P value lesser than 0.05. Further, for each sample the differential genes were ranked/scored using desiR package (Lazic et al, 2015). Differential genes were assigned score between 0-1, where 1 is highly significant and 0 being failed for the given criteria. Overall significance score was calculated based on a score from fold change, adjusted P value and base mean between contrasts with varying weightage of 100%, 100% and 50% respectively. To illustrate the simple comparison of differentially expressed genes across samples, the overlap of differentially expressed genes with fold change beyond ± 1 and adjusted P values < 0.05 is shown in Figure 7. To elucidate the effect of DrpinMyc treatment, the expression of genes coding for several transcription factors that are critical for regulatory mechanisms were further investigated. In this regard, a subset of the DE gene list was analysed, which was limited to genes that are coding for several TFs retrieved from ChEA database. This data demonstrates differentially expressing TF coding genes separately. The inventors assessed the common and unique differentially expressed transcription factors across all the comparisons (Figures 8 and 9). The ChEA 2016 database (Lachmann A, 2010) was used as a reference for analyzing the transcription factors that overlapped with that of the differential expression data. The ChEA 2016 version consists of 314 transcription factors. The inventors identified the intersecting genes between differentially expressed gene list and ChEA genes (TF coding genes). Results are split for up-and down-regulated genes (Table 1). Results The present Example revealed a number of genes were depleted in the DrpinMyc treated TNBC cells as compared to the mock treated cells (Figures 8 & 9). This RNAseq data further demonstrated that of the top twenty repressed transcripts with DrpinMyc treatment, 11 were known targets of Myc, 4 were known to regulate Myc and one was a target of another E-box transcription factor. The remainder have no known regulator at this time. The main repressed transcription factors were: E2F4, FOXM1, SUZ12 and EZH2. All are direct targets of c-Myc, except E2F4, which functions with Myc to drive certain genes. In conclusion, this data supports an on-target inhibitory effect on cMyc by the inhibitory hairpin oligonucleotide of DrpinMyc. Table 1. Summary statistics of differentially expressed transcription factors Example 3 Example 1 confirmed that DRpinMyc was capable of inhibiting cancer cell line growth in vitro. This Example tested whether this anti-cancer activity translated to in vivo xenograft cancer models in mice. Materials & Methods Triple-negative breast cancer (TNBC) patient-derived xenograft (PDX) model Seven week old female NOD-scid gamma (NSG) mice were grafted (3 ^rd mammary fat pad) with TNBC PDX tissue. When tumours reached an average size of 50 mm ³ , animals were treated with DRpin-Myc delivered by tail vein injection (1 injection per week for 6 weeks). Four doses of DRpin-Myc were tested (0, 1, 2.5, 5 mg/kg, 8 animals per dose). Tumour volumes (V=0.5 x length x width ² ) were normalised to determine the average percent change in tumour volume (tumour volume change (%) = (tumour volume Day x – tumour volume Day 0) / tumour volume Day 0 x 100). TNBC MDA-MB-231 xenograft model Seven week old female NOD-scid gamma (NSG) mice were injected (3 ^rd mammary fat pad) with 2.5 x 10 ⁶ MDA-MB-231 cells. When tumours reached an average size of 50 mm ³ , animals were treated with DRpin-Myc delivered by retro-orbital injection (2 injections per week for 4 weeks). Two doses of DRpin-Myc were tested (5 and 10 mg/kg, 6 animals per dose). Tumour volumes (V=0.5 x length x width ² ) were normalised to determine the average percent change in tumour volume (tumour volume change (%) = (tumour volume Day x – tumour volume Day 0) / tumour volume Day 0 x 100). Results A dose of 5 mg/kg of DRpin-Myc significantly reduced tumour growth in the TNBC PDX mouse model, without affecting weight gain in treated animals. Doses of 5 and 10 mg/kg of DRpin-Myc also significantly reduced tumour growth in the TNBC MDA-MB-231 xenograft mouse model. Example 4 This Example was performed to develop a model of DRpinMYC and the high-affinity DNA consensus sequence bound to the MYC:MAX complex and provide further data to develop the DRpin platform for controlled selectivity against transcription factors. Methods DRpinMYC model generation. The 2D structure dot-bracket notation was generated through the MC-Fold web server with default settings (Parisien & Major, 2008). The provided DRpinMYC hairpin sequence was 5'- GAGCACGUGGUUAAAAAACCACGUGCUC -3' (SEQ ID NO: 1). This notation was used to create 3D RNA models with RNA Composer (Biesiada, Purzycka, Szachniuk, Blazewicz, & Adamiak, 2016). PS linkages (*) with 2′-OMe (m) were added. RPPS or SPPS stereoisomers were chosen to represent the extreme ranges of structural dynamics imparted by the chirality of PS chemistry. DRpinMYC taking the form, 5′- mG*mA*mG*mC*mA*mC*mG*mU*mG*mG*mU*mU*mA*mA*mA*mA*mA*mA*mC *mC*mA*mC*mG*mU*mG*mC*mU*mC-3′. Conversion of the RNAComposer output to the RPPS and SPPS conformations was carried out using the alter command in PyMOL from Schrödinger, Inc (Schrödinger, L. & DeLano, W., 2020. PyMOL, Available at: http://www.pymol.org/pymol). The model of the high-affinity MYC DNA consensus sequence bound to the MYC:MAX complex was derived by mutating the bases within the duplex of the crystal structure RCSB PDB: 1NKP (Nair & Burley, 2003). Note that the crystal structure contains only the bHLH domains of both proteins. Bound models of DRpinMYC were generated using the MYC: MAX chains of 1NKP. The DNA duplex was removed, and the DRpinMYC models were translated to reproduce an essential interaction between MYC and the core CG of the E-box sequence 5′- CACGUG-3′ (SEQ ID NO: 12) (Nair & Burley, 2003). Generation of PS and 2′-OMe nucleotide force fields The standard RNA Amber force fields do not include parameters for the PS with 2′-OMe chemistry used herein. Thus, creating a force field library was necessary to represent the modified form of each nucleotide in both 5', 3' and central residues with both RP and SP PS stereoisomers. RESP charges for the library were generated in two runs with RED Server Development (Vanquelef et al., 2011). Partial charges are calculated by constructing the central 2′-OMe nucleotide in the C3′-endo geometry only, as the 2′-OMe is known to enhance this geometry. In calculating the PS charges, dimethyl phosphorothioate in both RP and SP enantiomers was also used in the run. The RESP-A1 method was chosen as this utilises the Hartree-Fock QM method with the 6-31G* basis set for Geometry Optimisation and Molecular Electrostatic Potential calculations in line with the method used to derive the original Amber RNA partial charges (Bayly, Cieplak, Cornell, & Kollman, 1993). Missing P-S bond and O2- P-S and OS-P-S angle parameters were derived from parm99 (Case et al., 2005; Cheatham, Cieplak, & Kollman, 1999). MD system creation Solvent dynamics of oligonucleotide-MYC: MAX systems were studied, and each system was generated with tleap from the AmberTools16 suite (Case et al., 2005). The DNAχOL15 force field was used to represent the DNA systems (Zgarbova et al., 2013; Zgarbova et al., 2011; Zgarbova et al., 2015). MYC and MAX residues were parameterized with the ff14SB protein force field (Maier et al., 2015). Explicit TIP3P water molecules were added to a padding distance of 17 Å in a box, and ionic strength NaCl was added to a concentration of 0.1 M (Mark & Nilsson, 2001). In addition to ionic strength, Na+ ions were added to neutralise the charge. All systems were solvated with ~33,000 water molecules, 100 Na+ and 80 Cl- ions. Oligonucleotide-MYC: MAX MD simulation All simulations were performed in triplicate using pmemd.cuda from the Amber 2020 package (Case et al., 2005; Salomon-Ferrer, Gotz, Poole, Le Grand, & Walker, 2013). Periodic boundary conditions were imposed in all directions. Hydrogen bonds were constrained with the SHAKE method, long-range electrostatic interactions were calculated with the Particle Mesh Ewald technique, and a non-bonded cut-off of 12 Å was used (Essmann et al., 1995; Ryckaert, Ciccotti, & Berendsen, 1977). The solvent and counterions were minimised using steepest descent for 10,000 steps and conjugate gradient for 5,000 steps. A time step of 2 fs was used throughout equilibration and production. After solvent minimisation, the solvent and counterions were heated from 0 to 300 °K over 50 ns of simulation by applying a 1 kcal/(mol•Å2) harmonic position restraint to the nucleotide heavy atoms with a constant number, volume and temperature (NVT) ensemble. The harmonic restraint was removed, and the system was minimised for 10,000 steps of steepest descent and 5,000 steps of conjugated gradient minimisation. The system was equilibrated by heating from 0 to 300 °K over 50 ns under the prior conditions. Production simulations were run at 300 °K using a Langevin thermostat with a collision frequency of 1.0 ps−1, constant pressure (NPT) at 1 atm, to a total production time frame of 2 μs. Coordinates, velocities, forces and energies were output every 10 ps or 5,000 steps. Trajectory Analysis Cpptraj from AmberTools 16 was used to analyse simulation trajectories (Roe & Cheatham, 2013). The analysis used all 200,000 production frames of each simulation, representing 6 μs of each oligonucleotide. RMSD to the original RNAcomposer models were calculated using all heavy or backbone atoms P, C5', O5', C4', C3', and O3'. K-means Clustering was calculated by sorting into two clusters based on intra-cluster RMSD measured via Davies-Bouldin Index and inter-cluster RMSD measured via pseudo-F. 3D structures were processed, and figures, along with buried surface area calculations, were generated with ChimeraX (Pettersen et al., 2021). MM/GBSA energetics and per residue decomposition. Free energies of binding were calculated with the MM/GBSA method using MMPBSA.py in Amber Tools 16 (Miller et al., 2012). These calculations were run under default parameters using all output trajectory frames from each simulation. The igb method 7 was used on recommendation by the Amber mailing list. idecomp=3 was used to perform pairwise decomposition. These calculations were read and processed using Notepad++ before being converted into heatmaps with the Matplotlib Python library (Hunter, 2007). MM/GBSA, or generalised Born and surface area continuum solvation, is a popular relative free energy of binding technique used to determine the strength by which a ligand binds a receptor. These energetics are typically calculated from molecular dynamics simulations of the receptor-ligand complex and are more thorough than empirical scoring methods. Ideally, the free energy difference of the binding interaction would be calculated as below (Genheden and Ryde, 2015). Where [A] represents the ligand in solvent and [B] represents the protein. Unfortunately, the energy contribution to binding would come mostly from solvent-solvent interactions, and the total energy would be far larger than the binding energy. [A]aq + [B] aq ^ [A*B*] aq* (1) In MM/GBSA, free energies are calculated through representative snapshots derived from a given system's molecular dynamics trajectories throughout a simulation. This method uses explicit or implicit solvation simulations with electrostatic contribution calculations to find the solvation free energy, using the Poisson-Boltzmann approach and the same approach to the non-polar solvation free energy to estimate the free energy of binding (Genheden and Ryde, 2015). This thermodynamic cycle is broadly defined by the below equation and visualised in Figure 12: ΔG solv, complex, ΔG solv, receptor, and ΔG solv, ligand is solvation free energies of the ligand-protein complex, the protein, and the ligand, respectively. Free energies are estimated using a continuum Poisson–Boltzmann/surface area approach (Genheden and Ryde, 2015). Results A larger E-box surface area strengthens DRpinMYC binding. From Figure 13, Each simulated system represents 6 μs of simulation time. All systems plateaued at ~3-4 Å within 50 ns; RMSD plots and a clustering summary are provided in Appendix A and B, respectively. The high-affinity MYC consensus sequence demonstrates the more compact arrangement of the B-form DNA geometry. In contrast, the DRpinMYC stereoisomers demonstrate the bulkier arrangement of the A-form geometry imparted by the 2′-OMe chemistry. Both the MYC and MAX basic region and the first helix of the bHLH domain bend to accommodate the backbone interactions of the bulkier DRpinMYC geometry compared to DNA. This bending is made possible by the loop region of the bHLH domain; this loop is largely disordered, allowing the first helix to pivot and impart more interactions between MYC and DRpinMYC than the DNA duplex. The combination of the bulkier A-form major groove of the DRpinMYC stereoisomers and the repositioning of the MYC helix imparts 350- 400 Å2 greater buried surface area between the ligand and complex when compared to DNA. Despite these differences, the interactions between each oligonucleotide and MYC: MAX are highly similar, with many basic amino acid contacts with the oligonucleotide backbone remaining unchanged. Van Der Waals and surface area drive DRpinMYC binding. Table 2. MM/GBSA free energies of binding table The MM/GBSA derived free binding energy was calculated from the oligonucleotide and MYC: MAX complex simulation trajectories and is provided in Table 2. Both stereoisomers of DRpinMYC demonstrate a clear decrease of -50 kcal/mol in binding energy and, thus, a far stronger interaction of DRpinMYC compared to the high-affinity DNA sequence. The Major driving force behind binding in both cases are electrostatic interactions between backbone PD or PS groups and the basic amino acids of the first helix of MYC and MAX. However, Evdw values demonstrate the greatest change in an individual value of -24 kcal/mol and align with the increased buried surface area in DRpinMYC systems. There is also a notable difference in Esurf, due to a greater surface area with which solvent-solute interaction may occur and is imparted by the bulkier DRpinMYC molecule. Thus, the increased buried surface area seen in Figure 13 imparts stronger or more Van Der Waal interactions between ligand and complex when compared to DNA, while the larger surface area also imparts more solvent-solute interactions. Despite different geometries, the pairwise interactions of the DNA duplex and the DRpinMYC stereoisomers are highly similar, as seen in Figure 14. There is little change in the MYC or MAX residues involved in binding, and electrostatic interactions between basic amino acids, such as Arginine or Lysine, and the oligonucleotide backbone still dominate. Some base interactions between MYC: MAX and DRpinMYC have shifted by 1-2 bases, and all interactions are more distributed than in the DNA duplex. The 5′ segment of the DRpinMYC hairpin represents the majority of interactions with MYC, while the 3′ segment interacts with MAX. Unlike the DNA duplex, the loop of DRpinMYC and the 5′ bases anterior to the E-box also contribute to the binding. The binding energy decomposition indicates that a similar complex is formed in both DRpinMYC and high-affinity DNA interactions. Discussion For this study, DRpinMYC stereoisomers were manually docked to the MYC: MAX complex, then solvated, simulated for several μs and compared to their DNA counterpart. Systems were analysed by K-means clustering, MM/GBSA and RMSD calculations. The data presented herein indicates that the MYC: MAX complex can bind to an A-form PS-linked hairpin of its high-affinity consensus sequence with a greater affinity than its DNA counterpart. The geometry of the A-form DRpinMYC and the B-form high-affinity DNA duplex differs. MM/GBSA calculations indicate that the MYC: MAX complex binds to DRpinMYC with a stronger affinity than the MYC DNA ligand. Van Der Waals interactions drive this increased affinity due to an increased major groove surface area. Although these interactions are more distributed, as indicated by energy decomposition, the simulation trajectories and clustering indicate that MYC is entirely capable of structural rearrangement to efficiently bind to an A- form geometry. DRpinMYC was partially unwound over the simulation time by its interaction with MYC: MAX. Similar local structural rearrangement is present in the DNA duplex bound to MYC: MAX in the original crystal structure (Nair & Burley, 2003) in which the backbone of the central CG bases of the E-box are pushed towards A-form phi and psi angles. References Adhikary, S., & Eilers, M. (2005). Transcriptional regulation and transformation by Myc proteins. Nat Rev Mol Cell Biol, 6(8), 635-645. doi:10.1038/nrm1703 Bayly, C. I., Cieplak, P., Cornell, W., & Kollman, P. A. (1993). A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model. The Journal of Physical Chemistry, 97(40), 10269-10280. doi:10.1021/j100142a004 Biesiada, M., Purzycka, K. J., Szachniuk, M., Blazewicz, J., & Adamiak, R. W. (2016). Automated RNA 3D Structure Prediction with RNAComposer. Methods Mol Biol, 1490, 199- 215. doi:10.1007/978-1-4939-6433-8_13 Cary, P. D., & Kneale, G. G. (2009). Circular dichroism for the analysis of protein-DNA interactions. Methods Mol Biol, 543, 613-624. doi:10.1007/978-1-60327-015-1_36 Case, D. A., Cheatham, T. E., 3rd, Darden, T., Gohlke, H., Luo, R., Merz, K. M., Jr., . . . Woods, R. J. (2005). The Amber biomolecular simulation programs. J Comput Chem, 26(16), 1668-1688. doi:10.1002/jcc.20290 Castell, A., Yan, Q., Fawkner, K., Hydbring, P., Zhang, F., Verschut, V., . .. Larsson, L. G. (2018). A selective high affinity MYC-binding compound inhibits MYC:MAX interaction and MYC-dependent tumor cell proliferation. Sci Rep, 8(1), 10064. doi:10.1038/s41598-018- 28107-4 Cheatham, T. E., 3rd, Cieplak, P., & Kollman, P. A. (1999). A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat. J Biomol Struct Dyn, 16(4), 845-862. doi:10.1080/07391102.1999.10508297 Choi, S. H., Mahankali, M., Lee, S. J., Hull, M., Petrassi, H. M., Chatterjee, A. K., ... Shen, W. (2017). Targeted Disruption of Myc-Max Oncoprotein Complex by a Small Molecule. ACS Chem Biol, 12(11), 2715-2719. doi:10.1021/acschembio.7b00799 Chou, K. M., Kukhanova, M., & Cheng, Y. C. (2000). A novel action of human apurinic/apyrimidinic endonuclease: excision of L-configuration deoxyribonucleoside analogs from the 3' termini of DNA. J Biol Chem, 275(40), 31009-31015. doi:10.1074/jbc.M004082200 Crooke, S. T., Seth, P. P., Vickers, T. A., & Liang, X. H. (2020). The Interaction of Phosphorothioate-Containing RNA Targeted Drugs with Proteins Is a Critical Determinant of the Therapeutic Effects of These Agents. J Am Chem Soc, 142(35), 14754-14771. doi:10.1021/jacs.0c04928 Dang, C. V. (2012). MYC on the path to cancer. Cell, 149(1), 22-35. doi:10.1016/j.cell.2012.03.003 Demma, M. J., Mapelli, C., Sun, A., Bodea, S., Ruprecht, B., Javaid, S., ... O'Neil, J. (2019). Omomyc Reveals New Mechanisms To Inhibit the MYC Oncogene. Mol Cell Biol, 39(22). doi:10.1128/MCB.00248-19 Dhanasekaran, R., Deutzmann, A., Mahauad-Fernandez, W. D., Hansen, A. S., Gouw, A. M., & Felsher, D. W. (2022). The MYC oncogene - the grand orchestrator of cancer growth and immune evasion. Nat Rev Clin Oncol, 19(1), 23-36. doi:10.1038/s41571-021-00549-2 Eckstein, F. (2014). Phosphorothioates, essential components of therapeutic oligonucleotides. Nucleic Acid Ther, 24(6), 374-387. doi:10.1089/nat.2014.0506 Essmann, U., Perera, L., Berkowitz, M. L., Darden, T., Lee, H., & Pedersen, L. G. (1995). A Smooth Particle Mesh Ewald Method. Journal of Chemical Physics, 103(19), 8577-8593. doi:Doi 10.1063/1.470117 Fiorentino, F. P., Tokgun, E., Sole-Sanchez, S., Giampaolo, S., Tokgun, O., Jauset, T., . . . Yokota, J. (2016). Growth suppression by MYC inhibition in small cell lung cancer cells with TP53 and RB1 inactivation. Oncotarget, 7(21), 31014-31028. doi:10.18632/oncotarget.8826 Hunter, J. D. (2007). Matplotlib: A 2D Graphics Environment. Computing in Science & Engineering, 9(3), 90-95. doi:10.1109/MCSE.2007.55 Janas, M. M., Jiang, Y., Schlegel, M. K., Waldron, S., Kuchimanchi, S., & Barros, S. A. (2017). Impact of Oligonucleotide Structure, Chemistry, and Delivery Method on In Vitro Cytotoxicity. Nucleic Acid Ther, 27(1), 11-22. doi:10.1089/nat.2016.0639 Llombart, V., & Mansour, M. R. (2022). Therapeutic targeting of "undruggable" MYC. EBioMedicine, 75, 103756. doi:10.1016/j.ebiom.2021.103756 Lourenco, C., Resetca, D., Redel, C., Lin, P., MacDonald, A. S., Ciaccio, R., ... Penn, L. Z. (2021). MYC protein interactors in gene transcription and cancer. Nat Rev Cancer, 21(9), 579- 591. doi:10.1038/s41568-021-00367-9 Maier, J. A., Martinez, C., Kasavajhala, K., Wickstrom, L., Hauser, K. E., & Simmerling, C. (2015). ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB. J Chem Theory Comput, 11(8), 3696-3713. doi:10.1021/acs.jctc.5b00255 Mark, P., & Nilsson, L. (2001). Structure and Dynamics of the TIP3P, SPC, and SPC/E Water Models at 298 K. The Journal of Physical Chemistry A, 105(43), 9954-9960. doi:10.1021/jp003020w Migawa, M. T., Shen, W., Wan, W. B., Vasquez, G., Oestergaard, M. E., Low, A., ... Seth, P. P. (2019). Site-specific replacement of phosphorothioate with alkyl phosphonate linkages enhances the therapeutic profile of gapmer ASOs by modulating interactions with cellular proteins. Nucleic Acids Res, 47(11), 5465-5479. doi:10.1093/nar/gkz247 Nair, S. K., & Burley, S. K. (2003). X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors. Cell, 112(2), 193-205. doi:10.1016/s0092-8674(02)01284-9 Niu, Z., Liu, H., Zhou, M., Wang, H., Liu, Y., Li, X., ... Li, G. (2015). Knockdown of c-Myc inhibits cell proliferation by negatively regulating the Cdk/Rb/E2F pathway in nasopharyngeal carcinoma cells. Acta Biochim Biophys Sin (Shanghai), 47(3), 183-191. doi:10.1093/abbs/gmu129 Papoulas, O., Williams, N. G., & Kingston, R. E. (1992). DNA binding activities of c-Myc purified from eukaryotic cells. J Biol Chem, 267(15), 10470-10480. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/1587829 Parisien, M., & Major, F. (2008). The MC-Fold and MC-Sym pipeline infers RNA structure from sequence data. Nature, 452(7183), 51-55. doi:10.1038/nature06684 Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., . . . Ferrin, T. E. (2021). UCSF ChimeraX: Structure visualization for researchers, educators, and developers. Protein Sci, 30(1), 70-82. doi:10.1002/pro.3943 Riniker, S. (2018). Fixed-Charge Atomistic Force Fields for Molecular Dynamics Simulations in the Condensed Phase: An Overview. J Chem Inf Model, 58(3), 565-578. doi:10.1021/acs.jcim.8b00042 Roe, D. R., & Cheatham, T. E., 3rd. (2013). PTRAJ and CPPTRAJ: Software for Processing and Analysis of Molecular Dynamics Trajectory Data. J Chem Theory Comput, 9(7), 3084- 3095. doi:10.1021/ct400341p Ryckaert, J.-P., Ciccotti, G., & Berendsen, H. J. C. (1977). Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. Journal of Computational Physics, 23(3), 327-341. doi:https://doi.org/10.1016/0021- 9991(77)90098-5 Sabit, H., Tombuloglu, H., Cevik, E., Abdel-Ghany, S., El-Zawahri, E., El-Sawy, A., ... Al- Suhaimi, E. (2021). Knockdown of c-MYC Controls the Proliferation of Oral Squamous Cell Carcinoma Cells in vitro via Dynamic Regulation of Key Apoptotic Marker Genes. Int J Mol Cell Med, 10(1), 45-55. doi:10.22088/IJMCM.BUMS.10.1.45 Salomon-Ferrer, R., Gotz, A. W., Poole, D., Le Grand, S., & Walker, R. C. (2013). Routine Microsecond Molecular Dynamics Simulations with AMBER on GPUs. 2. Explicit Solvent Particle Mesh Ewald. J Chem Theory Comput, 9(9), 3878-3888. doi:10.1021/ct400314y Shen, W., De Hoyos, C. L., Migawa, M. T., Vickers, T. A., Sun, H., Low, A., ... Crooke, S. T. (2019). Chemical modification of PS-ASO therapeutics reduces cellular protein-binding and improves the therapeutic index. Nat Biotechnol, 37(6), 640-650. doi:10.1038/s41587-019- Vanquelef, E., Simon, S., Marquant, G., Garcia, E., Klimerak, G., Delepine, J. C., . . . Dupradeau, F. Y. (2011). R.E.D. Server: a web service for deriving RESP and ESP charges and building force field libraries for new molecules and molecular fragments. Nucleic Acids Res, 39(Web Server issue), W511-517. doi:10.1093/nar/gkr288 Walhout, A. J., Gubbels, J. M., Bernards, R., van der Vliet, P. C., & Timmers, H. T. (1997). c- Myc/Max heterodimers bind cooperatively to the E-box sequences located in the first intron of the rat ornithine decarboxylase (ODC) gene. Nucleic Acids Res, 25(8), 1493-1501. doi:10.1093/nar/25.8.1493 Wang, Y. H., Liu, S., Zhang, G., Zhou, C. Q., Zhu, H. X., Zhou, X. B., ... Xu, N. Z. (2005). Knockdown of c-Myc expression by RNAi inhibits MCF-7 breast tumor cells growth in vitro and in vivo. Breast Cancer Res, 7(2), R220-228. doi:10.1186/bcr975 Yoo, J., Winogradoff, D., & Aksimentiev, A. (2020). Molecular dynamics simulations of DNA-DNA and DNA-protein interactions. Curr Opin Struct Biol, 64, 88-96. doi:10.1016/j.sbi.2020.06.007 You, S., Lee, H. G., Kim, K., & Yoo, J. (2020). Improved Parameterization of Protein-DNA Interactions for Molecular Dynamics Simulations of PCNA Diffusion on DNA. J Chem Theory Comput, 16(7), 4006-4013. doi:10.1021/acs.jctc.0c00241 Zgarbova, M., Luque, F. J., Sponer, J., Cheatham, T. E., 3rd, Otyepka, M., & Jurecka, P. (2013). Toward Improved Description of DNA Backbone: Revisiting Epsilon and Zeta Torsion Force Field Parameters. J Chem Theory Comput, 9(5), 2339-2354. doi:10.1021/ct400154j Zgarbova, M., Otyepka, M., Sponer, J., Mladek, A., Banas, P., Cheatham, T. E., 3rd, & Jurecka, P. (2011). Refinement of the Cornell et al. Nucleic Acids Force Field Based on Reference Quantum Chemical Calculations of Glycosidic Torsion Profiles. J Chem Theory Comput, 7(9), 2886-2902. doi:10.1021/ct200162x Zgarbova, M., Sponer, J., Otyepka, M., Cheatham, T. E., 3rd, Galindo-Murillo, R., & Jurecka, P. (2015). Refinement of the Sugar-Phosphate Backbone Torsion Beta for AMBER Force Fields Improves the Description of Z- and B-DNA. J Chem Theory Comput, 11(12), 5723- 5736. doi:10.1021/acs.jctc.5b00716