Design, synthesis, and biological activity of novel factor Xa inhibitors: improving metabolic stability by S1 and S4 ligand modification

Bioorg Med Chem. 2006 Mar 1;14(5):1309-30. doi: 10.1016/j.bmc.2005.09.056. Epub 2005 Nov 2.

Abstract

Serine protease factor xa (fXa) inhibitor 1 showed good ex vivo anti-fXa activity upon oral administration in rats. However, it has been revealed that 1 had low metabolic stability against human liver microsomes. To improve the metabolic stability, we attempted to modify the S1 and S4 ligands of 1. These modifications resulted in compound 34b, which exhibited selective anti-fXa activity and excellent anti-coagulation activity.

MeSH terms

  • Administration, Oral
  • Animals
  • Anticoagulants / chemical synthesis
  • Anticoagulants / pharmacology*
  • Antithrombin III* / chemical synthesis
  • Antithrombin III* / metabolism
  • Antithrombin III* / pharmacology
  • Binding Sites
  • Blood Coagulation / drug effects*
  • Blood Coagulation Tests
  • Dose-Response Relationship, Drug
  • Drug Design
  • Humans
  • Ligands
  • Microsomes, Liver / metabolism
  • Peptides / chemistry*
  • Peptides / metabolism
  • Rats
  • Serine Proteinase Inhibitors / pharmacology*
  • Structure-Activity Relationship

Substances

  • Anticoagulants
  • Ligands
  • Peptides
  • Serine Proteinase Inhibitors
  • Antithrombin III