Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1945101 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2009 | 9 Pages |
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 α-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.
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Authors
David I. Fernandez, John D. Gehman, Frances Separovic,