Differential Interaction of Antimicrobial Peptides with Lipid Structures Studied by Coarse-Grained Molecular Dynamics Simulations
| Autor: | Ernesto E. Ambroggio, Gerardo D. Fidelio, M. Florencia Martini, Galo Ezequiel Balatti, Mónica Pickholz |
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| Rok vydání: | 2017 |
| Předmět: |
Models
Molecular 0301 basic medicine coarse-grain Molecular Conformation Pharmaceutical Science Peptide helicoidal peptides Analytical Chemistry purl.org/becyt/ford/1 [https] Molecular dynamics chemistry.chemical_compound Drug Discovery LIPID BILAYERS Lipid bilayer chemistry.chemical_classification Membrane Chemistry (miscellaneous) Phosphatidylcholines Molecular Medicine CIENCIAS NATURALES Y EXACTAS AUREIN Otras Ciencias Biológicas Antimicrobial peptides Molecular Dynamics Simulation Article Amphibian Proteins lcsh:QD241-441 Ciencias Biológicas 03 medical and health sciences lcsh:Organic chemistry aurein Amphiphile Molecule Computer Simulation COARSE-GRAIN Physical and Theoretical Chemistry purl.org/becyt/ford/1.6 [https] maculatin lipid bilayers molecular dynamics POPC HELICOIDAL PEPTIDES MACULATIN Organic Chemistry Crystallography 030104 developmental biology chemistry Biophysics MOLECULAR DYNAMICS Antimicrobial Cationic Peptides |
| Zdroj: | Molecules, Vol 22, Iss 10, p 1775 (2017) CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET Molecules; Volume 22; Issue 10; Pages: 1775 Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry |
| ISSN: | 1420-3049 |
| DOI: | 10.3390/molecules22101775 |
| Popis: | 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. Fil: Balatti, Galo Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Física de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Física de Buenos Aires; Argentina Fil: Ambroggio, Ernesto Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Martini, María Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Metabolismo del Fármaco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Metabolismo del Fármaco; Argentina Fil: Pickholz, Mónica Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Física de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Física de Buenos Aires; Argentina |
| Databáze: | OpenAIRE |
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