P-50 フィブロネクチン関連ペプチドの構造-活性相関(ポスター発表の部)

概要

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The Arg-Gly-Asp (RGD)-containing peptides are known to inhibit tumor progression and platelet aggregation. Tripeptide RGD is essential for binding to receptors (integrin) on the cell surface. We had reported that both RGDS and PASS had antiparallel locations in the cyclic peptide, FR-1, which exhibited high activity as a platelet aggregation inhibitor. H-Cys^1- Arg^2-Gly^3-Asp^4-Ser^5-Pro^6-Ala^7-Ser^8-Ser^9-Cys^<10>-OH:FR-1 In order to investigate the structure-biological activity relationship of FR-1, we designed and synthesized analogs of this cyclic peptide. From these studies, we made three novel discoveries. It may be noted that, (1) the hydroxy groups in Ser-Ser were necessary for the binding to the fibrinogen receptor; (2) side chain' repulsion between the amino acid residues at position 5 and 6 in FR-1 provided the suitable conformation for binding to the receptor; (3) the more hydrophobicity the cyclic peptide had, the higher its affinity was to the receptor.
1994-09-20