Discovery of (phenylureido)piperidinyl benzamides as prospective inhibitors of bacterial autolysin E from Staphylococcus aureus

J Enzyme Inhib Med Chem. 2018 Dec;33(1):1239-1247. doi: 10.1080/14756366.2018.1493474.

Abstract

Autolysin E (AtlE) is a cell wall degrading enzyme that catalyzes the hydrolysis of the β-1,4-glycosidic bond between the N-acetylglucosamine and N-acetylmuramic acid units of the bacterial peptidoglycan. Using our recently determined crystal structure of AtlE from Staphylococcus aureus and a combination of pharmacophore modeling, similarity search, and molecular docking, a series of (Phenylureido)piperidinyl benzamides were identified as potential binders and surface plasmon resonance (SPR) and saturation-transfer difference (STD) NMR experiments revealed that discovered compounds bind to AtlE in a lower micromolar range. (phenylureido)piperidinyl benzamides are the first reported non-substrate-like compounds that interact with this enzyme and enable further study of the interaction of small molecules with bacterial AtlE as potential inhibitors of this target.

Keywords: Autolysin E; SPR; STD NMR; glycoside hydrolase; virtual screening.

MeSH terms

  • Anti-Bacterial Agents / chemical synthesis
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology*
  • Dose-Response Relationship, Drug
  • Drug Discovery*
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology*
  • Microbial Sensitivity Tests
  • Models, Molecular
  • Molecular Structure
  • N-Acetylmuramoyl-L-alanine Amidase / antagonists & inhibitors*
  • N-Acetylmuramoyl-L-alanine Amidase / chemistry
  • N-Acetylmuramoyl-L-alanine Amidase / metabolism
  • Piperidines / chemical synthesis
  • Piperidines / chemistry
  • Piperidines / pharmacology*
  • Staphylococcus aureus / drug effects*
  • Staphylococcus aureus / enzymology
  • Structure-Activity Relationship

Substances

  • Anti-Bacterial Agents
  • Enzyme Inhibitors
  • Piperidines
  • N-Acetylmuramoyl-L-alanine Amidase

Grants and funding

The authors acknowledge the financial support from the Slovenian Research Agency [research core funding No. P1–0017, P1–0012, P1-0048 and J1-8145].