title: Membrane interactions of antimicrobial peptides from Australian frogs.
abstract: The membrane interactions of four antimicrobial peptides, aurein 1.2, citropin 1.1, maculatin 1.1 and caerin 1.1, isolated from Australian tree frogs, are reviewed. All four peptides are amphipathic alpha-helices with a net positive charge and range in length from 13 to 25 residues. Despite several similar sequence characteristics, these peptides compromise the integrity of model membrane bilayers via different mechanisms; the shorter peptides exhibit a surface interaction mechanism while the longer peptides may form pores in membranes.
authors.affiliation: School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne VIC 3010, Australia.
authors.forename: David I
authors.initials: DI
authors.lastname: Fernandez
authors.forename: John D
authors.initials: JD
authors.lastname: Gehman
authors.forename: Frances
authors.initials: F
authors.lastname: Separovic
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000737:chemistry / Q000494:pharmacology*; D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000494:pharmacology*; D001315:Australia; D002462:Cell Membrane / Q000187:drug effects*; D006801:Humans; D008051:Lipid Bilayers; D009682:Magnetic Resonance Spectroscopy; D011898:Ranidae
chemical_list: D029845:Amphibian Proteins; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers