Studies on the Molecular Basis of Collagen-Platelet Interaction and Synthesis of Peptides That Will Inhibit This Interaction.

摘要

Studies on the identification and localization of peptides derived from collagen that specifically bind with platelets,are reported. Like collagens,cyanide bromide (CB) peptides have to be in an aggregated form to cause platelet aggregation. The authors have obtained chymotryptic and tryptic digest of alpha 1 CB6. The resulting periods were isolated by column chromatography and temperature programs have been devised to effect their renaturation and fibrillogenesis. In addition,collagen was digested with tadpole collagenase,and the resulting two molecules,comprising 3/4and 1/4of tropocollagen respectively,were found to be devoid of platelet activity. This experiment indicates that the critical sequence inalpha 1 CB6resides at the NH2-terminal of this peptide. A collagen-sepharose affinity column has been synthesized and was found to be active with respect to platelets. Isolation of the collagen receptor from platelet membrane has been accomplished.