Targeting class A and C serine β-lactamases with a broad-spectrum boronic acid derivative

J Med Chem. 2014 Jun 26;57(12):5449-58. doi: 10.1021/jm5006572. Epub 2014 Jun 16.

Abstract

Production of β-lactamases (BLs) is the most widespread resistance mechanism adopted by bacteria to fight β-lactam antibiotics. The substrate spectrum of BLs has become increasingly broad, posing a serious health problem. Thus, there is an urgent need for novel BL inhibitors. Boronic acid transition-state analogues are able to reverse the resistance conferred by class A and C BLs. We describe a boronic acid analogue possessing interesting and potent broad-spectrum activity vs class A and C serine-based BLs. Starting from benzo(b)thiophene-2-boronic acid (BZBTH2B), a nanomolar non-β-lactam inhibitor of AmpC that can potentiate the activity of a third-generation cephalosporin against AmpC-producing resistant bacteria, we designed a novel broad-spectrum nanomolar inhibitor of class A and C BLs. Structure-based drug design (SBDD), synthesis, enzymology data, and X-ray crystallography results are discussed. We clarified the inhibitor binding geometry responsible for broad-spectrum activity vs serine-active BLs using double mutant thermodynamic cycle studies.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Bacterial Proteins / antagonists & inhibitors*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Boronic Acids / chemical synthesis
  • Boronic Acids / chemistry*
  • Crystallography, X-Ray
  • Drug Design
  • Drug Resistance, Bacterial*
  • Escherichia coli Proteins / chemistry
  • Hydrogen Bonding
  • Models, Molecular
  • Molecular Structure
  • Serine / metabolism*
  • Static Electricity
  • Thermodynamics
  • beta-Lactamase Inhibitors*
  • beta-Lactamases / chemistry
  • beta-Lactamases / metabolism

Substances

  • Bacterial Proteins
  • Boronic Acids
  • Escherichia coli Proteins
  • beta-Lactamase Inhibitors
  • Serine
  • CTX-M-9 protein, E coli
  • AmpC beta-lactamases
  • beta-Lactamases
  • beta-lactamase TEM-1

Associated data

  • PDB/4LEN