Proceedings of the National Academy of Sciences · 1989 · 290 citations · 34 references
Life SciencesBiochemistryBiophysicsBioenergeticsMolecular BiophysicsSignal TransductionAntimicrobial PeptidesEnergy MetabolismMembrane BioenergeticsMitochondrial BioenergeticsPeptide ChemistryRespiration InhibitionAntibacterial PeptidesAntimicrobial Peptide ActivityCationic Antimicrobial PeptidesCationic PeptidesEnergy Transduction In MembranesMembrane Disruption MechanismsMembrane Free Energy
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.
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Naoki Kamo, Makoto Muratsugu, Ruji Hongoh et al. · The Journal of Membrane Biology · 1979 · 957 citations
Synthetic Amphiphilic Peptide Models for Protein Ion Channels
J. D. Lear, Zelda R. Wasserman, W.F. DeGrado · Science · 1988 · 602 citations