Membrane interactions of antimicrobial peptides from Australian frogs

被引:84
作者
Fernandez, David I. [1 ]
Gehman, John D. [1 ]
Separovic, Frances [1 ]
机构
[1] Univ Melbourne, Sch Chem, Inst Bio21, Melbourne, Vic 3010, Australia
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2009年 / 1788卷 / 08期
基金
澳大利亚研究理事会;
关键词
Antimicrobial peptide; Model membrane; Peptide-lipid interaction; Pore formation; Solid-state NMR; HOST-DEFENSE PEPTIDES; TREE-FROG; SKIN GLANDS; LITORIA-GENIMACULATA; ANTIBIOTIC PEPTIDES; PART; ANTIBACTERIAL PEPTIDE; MACULATIN PEPTIDES; GRAMICIDIN-A; MECHANISM;
D O I
10.1016/j.bbamem.2008.10.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:1630 / 1638
页数:9
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