Hydrophobic attachment site for adhesion peptides

Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – 15 to 23 amino acid residues in defined sequence

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514 13, C07K 710, A61K 3702

Patent

active

051208296

ABSTRACT:
The invention provides a method of attaching peptides containing a biologically active site, for example RGD-containing adhesion peptides, to a solid surface through a hydrophobic domain, and peptides so attached. The hydrophobic domain can contain either hydrophobic amino acids, such as leucine, valine, isoleucine or phenylalanine, or fatty acids, such as, for example, myristic acid, palmitic acid, arachidic acid or other fatty acids. Additionally, spacers, such as amino acids, between the hydrophobic domain and the biologically active domain can improve the presentation of the biologically active site. Specific peptides of the invention include

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Ginsberg et al., Inhibition of Fibronectin Binding to Platelets by Proteolytic Fragments and Synthetic Peptides which Support Fibroblast Adhesion; The Journal of Biological Chemistry 260(7):3931-3936 (1985).
Martin G. Low, Biochemistry of the Glycosyl-Phosphatidylinositol Membrane Protein Anchors, Biochem. J., (1987), 244, pp. 1-13.
George Cross, Eukaryotic Protein Modification and Membrane Attachment via Phosphatidylinositol, Cell, (48), pp. 179-181, Jan. 30, 1987.
Rideout et al., Amphiphilic Cationic Peptide Mediate Cell Adhesion to Plastic Surfaces, J. Cellular Physiology, 124:365-371 (1985).

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