title: Antimicrobial peptides of frog skin.
abstract: A mechanism of action for frog skin antimicrobial peptides has been proposed, based on the amphipathic nature of the peptides when they contact bacterial surfaces. This results in anion channel formation and penetration of the membrane which allows efflux of OH- and uncoupling of respiration in the bacteria. The question of occurrence of human antimicrobial peptides analogous to those in frogs has not been answered but early studies indicate that Erspamer's prediction is correct.
authors.affiliation: Queen's University, Department of Biochemistry, Kingston, ON, Canada.
authors.forename: J H
authors.initials: JH
authors.lastname: Spencer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D000935:Antifungal Agents / Q000378:metabolism*; D023181:Antimicrobial Cationic Peptides; D054806:Magainins; D008969:Molecular Sequence Data; D010101:Oxygen Consumption / Q000187:drug effects; D010455:Peptides / Q000235:genetics / Q000494:pharmacology*; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D012867:Skin / Q000737:chemistry / Q000382:microbiology; D012879:Skin Physiological Phenomena; D029867:Xenopus Proteins; D014982:Xenopus laevis / Q000502:physiology*
chemical_list: D000900:Anti-Bacterial Agents; D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; D054806:Magainins; D010455:Peptides; D021382:Protein Sorting Signals; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus