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Document Type and Number:
WIPO Patent Application WO1991005036
Kind Code:
An absorbed protein-independent cell-adhesive surface is disclosed. The treated surface comprises a chemically derivatized material to which small peptides, having less than 12 amino acid residues and including YIGSR, RGD or REDV amino acid sequence are covalently linked to. The peptides of the present invention include a terminal glycine amino acid. Tresyl chloride activation of surface hydroxyl moieties provides the active surface sites by which a terminal glycine arm of a selected peptide attaches to form covalent bonds between the substrate and peptide. Peptides high with cell adhesive properties are bound in high efficiency. By way of example, surfaces which may be used in conjunction with the present invention include polymer, metal, and ceramic surfaces. The most preferred polymer surfaces include PHEMA and PET polymer surfaces, with the most preferred glass surfaces being glycophase glass. The present methods also include a pretreatment method which provides hydroxyl moieties to surfaces devoid of readily available hydroxyl moieties. The pretreatment, by way of example, comprises immersion of the surface in a mixture of formaldehyde and acetic acid. Methods of preparing the treated surfaces are also included in the present invention. Also included are surface-treated biomedical implant devices and cell culturing devices. The treated surface promotes an enhanced rate and an enhanced amount of cell adhesion to the surface, independent of media serum concentrations or other absorbed proteins. The treated surfaces of the present invention are thermally stable, reusable, peptide efficient (attached to surface only) and resistant to cell proteolysis. The invention further concerns polymeric substrates with a surface having physically interpenetrating water-soluble polymer chains, and methods for production thereof.

Application Number:
Publication Date:
May 16, 1991
Filing Date:
September 27, 1990
Export Citation:
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International Classes:
A61L27/00; A61L17/14; A61L27/22; A61L27/34; A61L29/04; A61L29/08; A61L31/04; A61L31/10; C07K17/08; C07K17/14; C12M3/00; C12N5/00; C12N5/07; C12N5/077; C12N5/079; C12N11/08; (IPC1-7): C12N5/00; A61L27/00; C07K17/02; C07K17/10; A61F2/00
Domestic Patent References:
Foreign References:
Other References:
Dialog Information Service, file 155: Medline 66-90/Nov, Medline Acc. No. 900343042, SP Massia et al: "Covalent surface immobilisation of arg-gly-asp and tyr-ile-gly-ser-arg containing peptides to well de- fined cell-adhesive substrates" & Anal Biochem jun 1990, 187(2), p 292-301, abstract
Dialog information Service, file 5: Biosis Previews 69-90/Nov, BIOSIS Acc. No. 39130827, S P Massia et al: "Covalently attached GRGD on polymer surfacespromotes biospecific adhesion on mammalin cells" & Goldstein, W. E., D. Dibiasio and H Pedersen (Ed.) Annals of the New York Academy of Sciences, vol 589.Biochemical Engineering: sixth conference, Santa Barbara, California, USA, October 2-7, 1988. XI + 715p. New York Academy of Sciences: NY, NY, USA, 0(0). 1990. 261-270
Dialog Information Service, file 351: WPI, WPI Acc. No.: 88-351056/49; & JP,A,63 264 069 (IDEMITSU KOSAN K K) 31 October 1988, abstract
Dialog Information Service, file 351: WPI, WPIAcc. No. 89-150594/20 & US,A, 7221982 (Y Yamada et al) 7 March 1989, abstract
Analytical Biochemistry, Vol. 172, 1988 B K Brandley et al.: "Covalent attachment of an Arg-Gly-Asp sequence peptide to derivatizable polyacrylamid surfaces: support of fibro- blast adhesion and long-term growth ",
Dialog Information Service, file 155 Medline 66-90/NOV, Medline Acc. No. 89380220, K Tashiro et al: "A synthetic peptide containing the IKVAV sequence from the A chain of Laminin mediates the cell attachment, migration and neurite outgrowth", & J Biol Chem sep 25 1989, 264(27) p16174-82, abstract.
The Journal of Cell biology, vol 103, no 6, pt 2 Dec 1986, M J Humphries et al: "Identification of an alternatively spliced site in human plasma fibro-nection that mediates celltypespecific adhesion", pages 2637-2647, see the entire article.
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