Discovery of azetidine based ene-amides as potent bacterial enoyl ACP reductase (FabI) inhibitors

Eur J Med Chem. 2014 Sep 12:84:382-94. doi: 10.1016/j.ejmech.2014.07.036. Epub 2014 Jul 11.

Abstract

A novel and potent series of ene-amides featuring azetidines has been developed as FabI inhibitors active against drug resistant Gram-positive pathogens particularly staphylococcal organisms. Most of the compounds from the series possessed excellent biochemical inhibition of Staphylococcus aureus FabI enzyme and whole cell activity against clinically relevant MRSA, MSSA and MRSE organisms which are responsible for significant morbidity and mortality in community as well as hospital settings. The binding mode of one of the leads, AEA16, in Escherichia coli FabI enzyme was determined unambiguously using X-ray crystallography. The lead compounds displayed good metabolic stability in mice liver microsomes and pharmacokinetic profile in mice. The in vivo efficacy of lead AEA16 has been demonstrated in a lethal murine systemic infection model.

Keywords: Antibacterial; Azetidine; Ene-amide; Enoyl ACP reductase; FabI inhibitor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amides / chemistry
  • Amides / metabolism
  • Amides / pharmacology*
  • Animals
  • Azetidines / chemistry*
  • Crystallography, X-Ray
  • Dose-Response Relationship, Drug
  • Drug Discovery*
  • Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) / metabolism*
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / metabolism
  • Enzyme Inhibitors / pharmacology*
  • Male
  • Mice
  • Microsomes, Liver / metabolism
  • Models, Molecular
  • Molecular Structure
  • Staphylococcus aureus / cytology
  • Staphylococcus aureus / enzymology*
  • Structure-Activity Relationship

Substances

  • Amides
  • Azetidines
  • Enzyme Inhibitors
  • azetidine
  • Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)