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Issue 15, 2018
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Antimicrobial action of the cationic peptide, chrysophsin-3: a coarse-grained molecular dynamics study

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Abstract

Antimicrobial peptides (AMPs) are small cationic proteins that are able to destabilize a lipid bilayer structure through one or more modes of action. In this study, we investigate the processes of peptide aggregation and pore formation in lipid bilayers and vesicles by the highly cationic AMP, Chrysophsin-3 (chrys-3), using coarse-grained molecular dynamics (CG-MD) simulations and potential of mean force calculations. We study long 50 μs simulations of chrys-3 at different concentrations, both at the surface of dipalmitoylphosphatidylcholine (DPPC) and palmitoyloleoylphosphatidylcholine (POPC) bilayers, and also interacting within the interior of the lipid membrane. We show that aggregation of peptides at the surface, leads to pronounced deformation of lipid bilayers, leading in turn to lipid protrusions for peptide : ligand ratios > 1 : 12. In addition, aggregation of chrys-3 peptides within the centre of a lipid bilayer leads to spontaneous formation of pores and aggregates. Both mechanisms of interaction are consistent with previously reported experimental data for chrys-3. Similar results are observed also in POPC vesicles and mixed lipid bilayers composed of the zwitterionic lipid palmitoyloleoylphosphatidylethanolamine (POPE) and the negatively charged lipid palmitoyloleoylphosphatidylglycerol (POPG). The latter are employed as models of the bacterial membrane of Escherichia coli.

Graphical abstract: Antimicrobial action of the cationic peptide, chrysophsin-3: a coarse-grained molecular dynamics study

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Publication details

The article was received on 01 Nov 2017, accepted on 10 Feb 2018 and first published on 29 Mar 2018


Article type: Paper
DOI: 10.1039/C7SM02152F
Citation: Soft Matter, 2018,14, 2796-2807
  • Open access: Creative Commons BY license
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    Antimicrobial action of the cationic peptide, chrysophsin-3: a coarse-grained molecular dynamics study

    A. Catte, M. R. Wilson, M. Walker and V. S. Oganesyan, Soft Matter, 2018, 14, 2796
    DOI: 10.1039/C7SM02152F

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