Optimization of the beta-aminoester class of factor Xa inhibitors. Part 2: Identification of FXV673 as a potent and selective inhibitor with excellent In vivo anticoagulant activity

Bioorg Med Chem Lett. 2002 Jun 17;12(12):1671-4. doi: 10.1016/s0960-894x(02)00213-5.

Abstract

Further optimization of the beta-aminoester class of factor Xa (fXa) inhibitors is described culminating in the identification of 9c (FXV673), a potent and selective factor Xa inhibitor with excellent in vivo anticoagulant activity. An X-ray structure of FXV673 bound to human fXa is also presented. Based on its selectivity, potent in vivo activity and favorable pre-clinical safety profile, FXV673 was selected for further development and is currently undergoing clinical trials.

MeSH terms

  • Anticoagulants / chemistry*
  • Anticoagulants / pharmacology*
  • Crystallography, X-Ray
  • Cyclic N-Oxides / chemistry*
  • Cyclic N-Oxides / pharmacology*
  • Esters
  • Factor Xa Inhibitors*
  • Humans
  • Models, Molecular
  • Molecular Structure
  • Pyridines / chemistry*
  • Pyridines / pharmacology*
  • Serine Proteinase Inhibitors / chemistry*
  • Serine Proteinase Inhibitors / pharmacology*

Substances

  • Anticoagulants
  • Cyclic N-Oxides
  • Esters
  • Factor Xa Inhibitors
  • Pyridines
  • Serine Proteinase Inhibitors
  • otamixaban