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A novel molecular design of thrombin receptor antagonist
T Fujita1, M Nakajima, Y Inoue
1Department of Molecular Chemistry, Graduate School of Science, Kyushu University, Fukuoka, Japan.
Bioorganic & Medicinal Chemistry Letters
|June 9, 1999
Abstract:
In a computer modeling of transmembrane domains of human thrombin receptor, Lys-158 was found near the ligand binding site. To capture this basic residue, analogs of peptide ligand containing a series of acidic amino acids were synthesized and assayed for human platelet aggregation, and Ser-(p-F)Phe-Aad(= alphaaminoadipic acid)-Leu-Arg-Asn-Pro-NH2 was found to be a potent antagonist.