Magainins and the disruption of membrane-linked free-energy transduction

Proc Natl Acad Sci U S A. 1989 Sep;86(17):6597-601. doi: 10.1073/pnas.86.17.6597.

Abstract

Magainins, a family of positively charged peptides, are partly if not wholly responsible for antimicrobial activity in skin extracts of Xenopus laevis. We report here that members of the magainin family--i.e., the 21-amino acid peptide PGLa and the 23-amino acid peptide magainin 2 amide (PGSa)--dissipate the electric potential across various energy-transducing membranes and thus uncouple respiration from other free-energy-requiring processes. We propose that this is a likely mechanism for the antimicrobial effects of these compounds.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Bacterial Agents / pharmacology
  • Antimicrobial Cationic Peptides*
  • Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone / pharmacology
  • Cell Membrane / drug effects
  • Cell Membrane / physiology*
  • Escherichia coli / physiology
  • Magainins
  • Male
  • Membrane Potentials / drug effects
  • Mitochondria, Liver / drug effects
  • Mitochondria, Liver / metabolism*
  • Oxidative Phosphorylation / drug effects
  • Peptides / pharmacology*
  • Rats
  • Rats, Inbred Strains
  • Xenopus Proteins*
  • Xenopus laevis

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Magainins
  • Peptides
  • Xenopus Proteins
  • peptide-Gly-Leu-amide
  • magainin 2 peptide, Xenopus
  • Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone