Design and structure-activity relationships of potent and selective inhibitors of blood coagulation factor Xa

J Med Chem. 1999 Sep 9;42(18):3557-71. doi: 10.1021/jm990040h.

Abstract

The discovery of a series of non-peptide factor Xa (FXa) inhibitors incorporating 3-(S)-amino-2-pyrrolidinone as a central template is described. After identifying compound 4, improvements in in vitro potency involved modifications of the liphophilic group and optimizing the angle of presentation of the amidine group to the S1 pocket of FXa. These studies ultimately led to compound RPR120844, a potent inhibitor of FXa (K(i) = 7 nM) which shows selectivity for FXa over trypsin, thrombin, and several fibrinolytic serine proteinases. RPR120844 is an effective anticoagulant in both the rat model of FeCl(2)-induced carotid artery thrombosis and the rabbit model of jugular vein thrombus formation.

MeSH terms

  • Animals
  • Anticoagulants / chemical synthesis*
  • Anticoagulants / pharmacology
  • Crystallography, X-Ray
  • Factor Xa Inhibitors*
  • Humans
  • Models, Molecular
  • Molecular Structure
  • Pyrrolidinones / chemical synthesis*
  • Pyrrolidinones / pharmacology
  • Rabbits
  • Rats
  • Serine Proteinase Inhibitors / chemical synthesis
  • Serine Proteinase Inhibitors / pharmacology
  • Stereoisomerism
  • Structure-Activity Relationship
  • Sulfonamides / chemical synthesis*
  • Sulfonamides / pharmacology
  • Thiophenes / chemical synthesis*
  • Thiophenes / pharmacology
  • Thrombosis / drug therapy

Substances

  • Anticoagulants
  • Factor Xa Inhibitors
  • Pyrrolidinones
  • RPR 120844
  • Serine Proteinase Inhibitors
  • Sulfonamides
  • Thiophenes