Structure-Based Design of Macrocyclic Factor XIa Inhibitors: Discovery of the Macrocyclic Amide Linker

J Med Chem. 2017 Feb 9;60(3):1060-1075. doi: 10.1021/acs.jmedchem.6b01460. Epub 2017 Jan 31.

Abstract

A novel series of macrocyclic FXIa inhibitors was designed based on our lead acyclic phenyl imidazole chemotype. Our initial macrocycles, which were double-digit nanomolar FXIa inhibitors, were further optimized with assistance from utilization of structure-based drug design and ligand bound X-ray crystal structures. This effort resulted in the discovery of a macrocyclic amide linker which was found to form a key hydrogen bond with the carbonyl of Leu41 in the FXIa active site, resulting in potent FXIa inhibitors. The macrocyclic FXIa series, exemplified by compound 16, had a FXIa Ki = 0.16 nM with potent anticoagulant activity in an in vitro clotting assay (aPTT EC1.5x = 0.27 μM) and excellent selectivity against the relevant blood coagulation enzymes.

Publication types

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

MeSH terms

  • Amides / chemistry*
  • Drug Discovery
  • Factor XIa / antagonists & inhibitors*
  • Hydrogen Bonding
  • Ligands
  • Macrocyclic Compounds / chemistry
  • Macrocyclic Compounds / pharmacokinetics
  • Macrocyclic Compounds / pharmacology*
  • Molecular Structure
  • Serine Proteinase Inhibitors / chemistry*
  • Serine Proteinase Inhibitors / pharmacokinetics
  • Serine Proteinase Inhibitors / pharmacology*

Substances

  • Amides
  • Ligands
  • Macrocyclic Compounds
  • Serine Proteinase Inhibitors
  • Factor XIa