期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1808, 期 9, 页码 2197-2205出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2011.05.001
关键词
Antimicrobial peptide; Peptide-membrane interaction; Molecular dynamics; Peptide folding; Structure-function of cyclic peptide
资金
- Spanish MICINN [MAT2008-04834]
- MEC [BES-2006-11671]
- Netherlands NWO
- BBSRC
- NWO [700.56302]
- Zernike Institute for Advanced Materials
We report the molecular basis for the differences in activity of cyclic and linear antimicrobial peptides. We iteratively performed atomistic molecular dynamics simulations and biophysical measurements to probe the interaction of a cyclic antimicrobial peptide and its inactive linear analogue with model membranes. We establish that, relative to the linear peptide, the cyclic one binds stronger to negatively charged membranes. We show that only the cyclic peptide folds at the membrane interface and adopts a beta-sheet structure characterised by two turns. Subsequently, the cyclic peptide penetrates deeper into the bilayer while the linear peptide remains essentially at the surface. Finally, based on our comparative study, we propose a model characterising the mode of action of cyclic antimicrobial peptides. The results provide a chemical rationale for enhanced activity in certain cyclic antimicrobial peptides and can be used as a guideline for design of novel antimicrobial peptides. (C) 2011 Elsevier B.V. All rights reserved.
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