作者
Chrystalleni Hadjicharalambous, Tania Sheynis, Raz Jelinek, Michael T Shanahan, Andre J Ouellette, Electra Gizeli
发表日期
2008/11/25
期刊
Biochemistry
卷号
47
期号
47
页码范围
12626-12634
出版商
American Chemical Society
简介
Mammalian α-defensins all have a conserved triple-stranded β-sheet structure that is constrained by an invariant tridisulfide array, and the peptides exert bactericidal effects by permeabilizing the target cell envelope. Curiously, the disordered, disulfide-null variant of mouse α-defensin cryptdin-4 (Crp4), termed (6C/A)-Crp4, has bactericidal activity equal to or greater than that of the native peptide, providing a rationale for comparing the mechanisms by which the peptides interact with and disrupt phospholipid vesicles of defined composition. For both live Escherichia coli ML35 cells and model membranes, disordered (6C/A)-Crp4 induced leakage in a manner similar to that of Crp4 but had less overall membrane permeabilizing activity. Crp4 induction of the leakage of the fluorophore from electronegative liposomes was strongly dependent on vesicle lipid charge and composition, and the incorporation of cardiolipin …
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C Hadjicharalambous, T Sheynis, R Jelinek… - Biochemistry, 2008