Publication: Membrane association and selectivity of the antimicrobial peptide NK-2: A molecular dynamics simulation study
Issued Date
2009-09-01
Resource Type
ISSN
10991387
10752617
10752617
DOI
Other identifier(s)
2-s2.0-70449647113
Rights
Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Peptide Science. Vol.15, No.10 (2009), 654-667
Suggested Citation
Jutarat Pimthon, Regine Willumeit, Andreas Lendleina, Dieter Hofmann Membrane association and selectivity of the antimicrobial peptide NK-2: A molecular dynamics simulation study. Journal of Peptide Science. Vol.15, No.10 (2009), 654-667. doi:10.1002/psc.1165 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/27149
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Title
Membrane association and selectivity of the antimicrobial peptide NK-2: A molecular dynamics simulation study
Abstract
In an effort to better understand the initial mechanism of selectivity and membrane association of the synthetic antimicrobial peptide NK-2, we have applied molecular dynamics simulation techniques to elucidate the interaction of the peptide with the membrane interfaces. A homogeneous dipalmitoylphosphatidylglycerol (DPPG) and a homogeneous dipalmitoylphosphatidylethanolamine (DPPE) bilayers were taken as model systems for the cytoplasmic bacterial and human erythrocyte membranes, respectively. The results of our simulations on DPPG and DPPE model membranes in the gel phase show that the binding of the peptide, which is considerably stronger for the negatively charged DPPG lipid bilayer than for the zwitterionic DPPE, ismostly governed by electrostatic interactions between negatively charged residues in the membrane and positively charged residues in the peptide. In addition, a characteristic distribution of positively charged residues along the helix facilitates a peptide orientation parallel to the membrane interface. Once the peptides reside close to the membrane surface of DPPG with the more hydrophobic side chains embedded into the membrane interface, the peptide initially disturbs the respective bilayer integrity by a decrease of the order parameter of lipid acyl chain close to the head group region, and by a slightly decrease in bilayer thickness. We found that the peptide retains a high content of helical structure on the zwitterionic membrane-water interface, while the loss of α-helicity is observed within a peptide adsorbed onto negatively charged lipid membranes. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.