Structure-based drug design of pyrazinone antithrombotics as selective inhibitors of the tissue factor VIIa complex

Bioorg Med Chem Lett. 2003 Jul 21;13(14):2319-25. doi: 10.1016/s0960-894x(03)00410-4.

Abstract

Structure-based drug design coupled with polymer-assisted solution-phase library synthesis was utilized to develop a series of pyrazinone inhibitors of the tissue factor/Factor VIIa complex. The crystal structure of a tri-peptide ketothiazole complexed with TF/VIIa was utilized in a docking experiment that identified a benzyl-substituted pyrazinone as a P(2) surrogate for the tri-peptide. A 5-step PASP library synthesis of these aryl-substituted pyrazinones was developed. The sequence allows for attachment of a variety of P(1) and P(3) moieties, which led to synthesis pyrazinone 23. Compound 23 exhibited 16 nM IC(50) against TF/VIIa with >6250x selectivity versus Factor Xa and thrombin. This potent and highly selective inhibitor of TF/VIIa was chosen for pre-clinical intravenous proof-of-concept studies to demonstrate the separation between antithrombotic efficacy and bleeding side effects in a primate model of thrombosis.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Crystallography, X-Ray
  • Drug Design
  • Factor VIIa / antagonists & inhibitors*
  • Factor Xa Inhibitors
  • Fibrinolytic Agents / chemical synthesis*
  • Fibrinolytic Agents / pharmacology*
  • Indicators and Reagents
  • Models, Molecular
  • Molecular Conformation
  • Peptide Library
  • Prothrombin / antagonists & inhibitors
  • Pyrazines / chemical synthesis*
  • Pyrazines / pharmacology*
  • Structure-Activity Relationship
  • Thrombin / antagonists & inhibitors
  • Thrombosis / blood
  • Thrombosis / chemically induced
  • Trypsin Inhibitors / chemical synthesis
  • Trypsin Inhibitors / pharmacology

Substances

  • Factor Xa Inhibitors
  • Fibrinolytic Agents
  • Indicators and Reagents
  • Peptide Library
  • Pyrazines
  • Trypsin Inhibitors
  • Prothrombin
  • Factor IIa
  • Factor VIIa
  • Thrombin