Structural study of phenyl boronic acid derivatives as AmpC beta-lactamase inhibitors

Bioorg Med Chem Lett. 2010 Jun 1;20(11):3416-9. doi: 10.1016/j.bmcl.2010.04.007. Epub 2010 Apr 9.


A small set of boronic acids acting as low nanomolar inhibitors of AmpC beta-lactamase were designed and synthesized in the effort to improve affinity, pharmacokinetic properties, and to provide a valid lead compound. X-ray crystallography revealed the binary complex of the best inhibitor bound to the enzyme, highlighting possibilities for its further rational derivatization and chemical optimization.

Publication types

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

MeSH terms

  • Bacterial Proteins / antagonists & inhibitors*
  • Boronic Acids / chemistry
  • Boronic Acids / pharmacology*
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology*
  • Models, Molecular
  • Protein Conformation
  • beta-Lactamase Inhibitors*
  • beta-Lactamases


  • Bacterial Proteins
  • Boronic Acids
  • Enzyme Inhibitors
  • beta-Lactamase Inhibitors
  • AmpC beta-lactamases
  • beta-Lactamases
  • benzeneboronic acid