Structure-Based Design of Macrocyclic Coagulation Factor VIIa Inhibitors

J Med Chem. 2015 Aug 13;58(15):6225-36. doi: 10.1021/acs.jmedchem.5b00788. Epub 2015 Jul 28.

Abstract

On the basis of a crystal structure of a phenylpyrrolidine lead and subsequent molecular modeling results, we designed and synthesized a novel series of macrocyclic FVIIa inhibitors. The optimal 16-membered macrocycle was 60-fold more potent than an acyclic analog. Further potency optimization by incorporation of P1' alkyl sulfone and P2 methyl groups provided a macrocycle with TF/FVIIa Ki = 1.6 nM, excellent selectivity against a panel of seven serine proteases, and FVII-deficient prothrombin time EC2x = 1.2 μM. Discovery of this potent, selective macrocyclic scaffold opens new possibilities for the development of orally bioavailable FVIIa inhibitors.

MeSH terms

  • Drug Design
  • Factor VIIa / antagonists & inhibitors*
  • Macrocyclic Compounds / chemistry
  • Macrocyclic Compounds / pharmacology
  • Models, Molecular
  • Molecular Structure
  • Serine Proteinase Inhibitors / chemistry*
  • Serine Proteinase Inhibitors / pharmacology*

Substances

  • Macrocyclic Compounds
  • Serine Proteinase Inhibitors
  • Factor VIIa

Associated data

  • PDB/4ZXX
  • PDB/4ZXY