A novel molecular design of thrombin receptor antagonist

Tsugumi Fujita, Masahide Nakajima, Yoshihisa Inoue, Takeru Nose, Yasuyuki Shimohigashi

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


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(= α-aminoadipic acid)-Leu-Arg-Asn-Pro-NH2 was found to be a potent antagonist.

Original languageEnglish
Pages (from-to)1351-1356
Number of pages6
JournalBioorganic and Medicinal Chemistry Letters
Issue number10
Publication statusPublished - May 17 1999

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry


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