Skip to main content

Research Repository

Advanced Search

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

Catte, Andrea; Wilson, Mark R.; Walker, Martin; Oganesyan, Vasily S.

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


Andrea Catte

Martin Walker

Vasily S. Oganesyan


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.

Journal Article Type Article
Acceptance Date Feb 10, 2018
Online Publication Date Mar 29, 2018
Publication Date Apr 21, 2018
Deposit Date Feb 15, 2018
Publicly Available Date Feb 15, 2018
Journal Soft Matter
Print ISSN 1744-683X
Electronic ISSN 1744-6848
Publisher Royal Society of Chemistry
Peer Reviewed Peer Reviewed
Volume 14
Issue 15
Pages 2796-2807
Public URL


You might also like

Downloadable Citations