1990 Volume 19 Issue 3 Pages 1078-1082
In extracorporeal circuration, platelet aggregation and adhesion to materials were mediated by adhesive proteins. RGD (Arg-Gly-Asp)-peptides which is the fragment of adhesive proteins inhibit the binding of activated platelets to adhesive proteins. Based on NMR and CD conformational analyses, spacial orientation of Arg and Asp residues was found to be a principal determinant for binding of peptides to platelet receptors. Rigid spacial orientation with high activity was achieved by enhancement of β-turn like intramolecular hydrogen bonding and cyclization of peptide skeleton. Oligopeptides obtained showed dose-dependent inhibition of platelet aggregation. These compounds will be applicable as a novel platelet-preserving agent in extracorporeal circuration.