Noncovalent thrombin inhibitors incorporating an imidazolylethynyl P1

Bioorg Med Chem Lett. 2000 Dec 18;10(24):2775-8. doi: 10.1016/s0960-894x(00)00579-5.

Abstract

A series of noncovalent tripeptidic thrombin inhibitors incorporating a unidazolylethynyl moiety at P1 was investigated. A number of compounds of this series were highly potent and selective versus trypsin, and several compounds demonstrated good oral absorption in rats (F = 58% for compound 19).

Publication types

  • Comparative Study

MeSH terms

  • Acetylene / chemical synthesis
  • Acetylene / pharmacology
  • Alkynes / chemical synthesis
  • Alkynes / metabolism*
  • Animals
  • Cattle
  • Hemostatics / antagonists & inhibitors
  • Hemostatics / metabolism
  • Humans
  • Imidazoles / chemical synthesis
  • Imidazoles / metabolism*
  • Imidazoles / pharmacology*
  • Models, Molecular
  • Protein Binding
  • Serine Proteinase Inhibitors / chemical synthesis*
  • Serine Proteinase Inhibitors / pharmacology
  • Structure-Activity Relationship
  • Thrombin / antagonists & inhibitors*
  • Thrombin / metabolism
  • Trypsin / metabolism

Substances

  • Alkynes
  • Hemostatics
  • Imidazoles
  • Serine Proteinase Inhibitors
  • Trypsin
  • Thrombin
  • Acetylene