Next Article in Journal
Phytotherapeutics: The Emerging Role of Intestinal and Hepatocellular Transporters in Drug Interactions with Botanical Supplements
Next Article in Special Issue
Phospholipids of Animal and Marine Origin: Structure, Function, and Anti-Inflammatory Properties
Previous Article in Journal
Protective Effect of Flavonoids from Ziziphus jujuba cv. Jinsixiaozao against Acetaminophen-Induced Liver Injury by Inhibiting Oxidative Stress and Inflammation in Mice
Previous Article in Special Issue
Bioactivity In Vitro of Quercetin Glycoside Obtained in Beauveria bassiana Culture and Its Interaction with Liposome Membranes
Article Menu
Issue 10 (October) cover image

Export Article

Open AccessArticle
Molecules 2017, 22(10), 1775;

Differential Interaction of Antimicrobial Peptides with Lipid Structures Studied by Coarse-Grained Molecular Dynamics Simulations

Departamento de Física, Facultad de Ciencias Exactas y Naturales, CONICET-Universidad de Buenos Aires, IFIBA, Buenos Aires C1428BFA, Argentina
Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC), Departamento de Química Biológica “Dr. Ranwel Caputto”, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Córdoba X500HUA, Argentina
Departamento de Farmacología, Instituto de la Química y Metabolismo del Fármaco (IQUIMIFA), Facultad de Farmacia y Bioquímica, Cátedra de Química Medicinal, CONICET-Universidad de Buenos Aires, Buenos Aires C1113AAD, Argentina
Author to whom correspondence should be addressed.
Received: 30 August 2017 / Accepted: 17 October 2017 / Published: 20 October 2017
(This article belongs to the Special Issue Phospholipids: Structure and Function)
Full-Text   |   PDF [7976 KB, uploaded 20 October 2017]   |  


In this work; we investigated the differential interaction of amphiphilic antimicrobial peptides with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) lipid structures by means of extensive molecular dynamics simulations. By using a coarse-grained (CG) model within the MARTINI force field; we simulated the peptide–lipid system from three different initial configurations: (a) peptides in water in the presence of a pre-equilibrated lipid bilayer; (b) peptides inside the hydrophobic core of the membrane; and (c) random configurations that allow self-assembled molecular structures. This last approach allowed us to sample the structural space of the systems and consider cooperative effects. The peptides used in our simulations are aurein 1.2 and maculatin 1.1; two well-known antimicrobial peptides from the Australian tree frogs; and molecules that present different membrane-perturbing behaviors. Our results showed differential behaviors for each type of peptide seen in a different organization that could guide a molecular interpretation of the experimental data. While both peptides are capable of forming membrane aggregates; the aurein 1.2 ones have a pore-like structure and exhibit a higher level of organization than those conformed by maculatin 1.1. Furthermore; maculatin 1.1 has a strong tendency to form clusters and induce curvature at low peptide–lipid ratios. The exploration of the possible lipid–peptide structures; as the one carried out here; could be a good tool for recognizing specific configurations that should be further studied with more sophisticated methodologies. View Full-Text
Keywords: maculatin; aurein; helicoidal peptides; lipid bilayers; molecular dynamics; coarse-grain maculatin; aurein; helicoidal peptides; lipid bilayers; molecular dynamics; coarse-grain

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Balatti, G.E.; Ambroggio, E.E.; Fidelio, G.D.; Martini, M.F.; Pickholz, M. Differential Interaction of Antimicrobial Peptides with Lipid Structures Studied by Coarse-Grained Molecular Dynamics Simulations. Molecules 2017, 22, 1775.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top