Open AccessMagainins and the disruption of membrane-linked free-energy transduction.
Author(s) -
Hans V. Westerhoff,
Davor Juretić,
Richard W. Hendler,
Michael Zasloff
Publication year - 1989
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.17.6597
Subject(s) - magainin , xenopus , peptide , antimicrobial peptides , amino acid , membrane , antimicrobial , chemistry , biophysics , biochemistry , biology , organic chemistry , gene
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.