Design, synthesis and SAR of RGD peptide hybrids as highly efficient inhibitors of platelet aggregation

A new series of peptide hybrids is developed as highly potent and selective antagonists of the GPIIb/IIIa receptor through rational modification of the RGDX sequence. Structure-activity relationships of these peptide hybrids have disclosed the important role of the C-terminal hydrophobic moiety and the N-terminal arginine side chain surrogates. Molecular modeling study strongly suggests the significance of a γ-turn conformation to achieve exceedingly high activity and receptor specificity.