Membrane interactions of antimicrobial peptides from Australian frogs.
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.
Fernandez
David I
DI
School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne VIC 3010, Australia.
Gehman
John D
JD
Separovic
Frances
F
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
D029845:Amphibian Proteins; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers