Substituted thiophene-anthranilamides as potent inhibitors of human factor Xa

Bioorg Med Chem. 2007 Mar 1;15(5):2127-46. doi: 10.1016/j.bmc.2006.12.019. Epub 2006 Dec 13.

Abstract

A series of thiophene-containing non-amidine factor Xa inhibitors is described. Simple methyl-substituted thiophene analogs were relatively weak inhibitors. However, introduction of hydrophilic substituents at C-4 or C-5 of the thiophene afforded inhibitors with low nanomolar potency. Optimization of the thiophene substituent at C-4 afforded subnanomolar inhibitors with improved in vitro anticoagulant activity. Incorporating basic amine substituents on the thiophene increased hydrophilicity and improved anticoagulant activity. The pharmacokinetic profile of one inhibitor was evaluated in dogs, and the X-ray crystal structure of this compound bound to factor Xa provides insight into the observed SAR for binding to factor Xa.

MeSH terms

  • Amides / chemistry
  • Amides / pharmacology*
  • Animals
  • Crystallography, X-Ray
  • Dogs
  • Factor Xa Inhibitors*
  • Humans
  • Magnetic Resonance Spectroscopy
  • Male
  • Models, Molecular
  • Serine Proteinase Inhibitors / pharmacokinetics
  • Serine Proteinase Inhibitors / pharmacology*
  • Structure-Activity Relationship
  • Thiophenes / chemistry*

Substances

  • Amides
  • Factor Xa Inhibitors
  • Serine Proteinase Inhibitors
  • Thiophenes