An antimicrobial bicyclic peptide from chemical space against multidrug resistant Gram-negative bacteria

Chem Commun (Camb). 2018 May 15;54(40):5130-5133. doi: 10.1039/c8cc02412j.

Abstract

We used the concept of chemical space to explore a virtual library of bicyclic peptides formed by double thioether cyclization of a precursor linear peptide, and identified an antimicrobial bicyclic peptide (AMBP) with remarkable activity against several MDR strains of Acinetobacter baumannii and Pseudomonas aeruginosa.

MeSH terms

  • Acinetobacter baumannii / drug effects
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology*
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / pharmacology*
  • Bacillus subtilis / drug effects
  • Biofilms / drug effects
  • Cell Membrane / drug effects
  • Drug Evaluation, Preclinical / methods
  • Drug Resistance, Multiple, Bacterial / drug effects*
  • Humans
  • Microbial Sensitivity Tests
  • Molecular Dynamics Simulation
  • Peptides, Cyclic / chemistry
  • Peptides, Cyclic / pharmacology*
  • Protein Structure, Secondary
  • Pseudomonas aeruginosa / drug effects
  • Small Molecule Libraries / chemistry
  • Small Molecule Libraries / pharmacology

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Peptides, Cyclic
  • Small Molecule Libraries