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