Modified thrombin receptor-agonist peptide ligands. Synthesis and conformational analysis of analogs of the N-terminal tripeptide region

Analogs 2–24 of the N-terminal tripeptide region of the tethered peptide ligand for human thrombin receptor have been synthesized for elucidation of the receptor bound conformation of the ligand peptide and the conformational analysis of model structures 25–30 of those peptide analogs suggested a plausible conformation for the receptor bound structure of the tripeptide region. Abstract Analogs of the N-terminal tripeptide region of the tethered peptide ligand for human thrombin receptor have been synthesized and the conformational analysis of model structures of those peptide analogs suggested a plausible conformation for the receptor bound structure of the tripeptide region.