Differential interaction of antimicrobial peptides with lipid structures studied by coarse-grained molecular dynamics simulations

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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Balatti, G.E., Ambroggio, E.E., Fidelio, G.D., Martini, M.F., Pickholz, M.
Formato:	JOUR
Materias:	Aurein Coarse-grain Helicoidal peptides Lipid bilayers Maculatin Molecular dynamics 1-palmitoyl-2-oleoylphosphatidylcholine amphibian protein antimicrobial cationic peptide aurein 1.2 peptide maculatin-1.1 protein, Litoria phosphatidylcholine chemistry computer simulation conformation lipid bilayer metabolism molecular dynamics molecular model Amphibian Proteins Antimicrobial Cationic Peptides Computer Simulation Lipid Bilayers Models, Molecular Molecular Conformation Molecular Dynamics Simulation Phosphatidylcholines
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_14203049_v22_n10_p_Balatti
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_14203049_v22_n10_p_Balatti
record_format	dspace
spelling	todo:paper_14203049_v22_n10_p_Balatti2023-10-03T16:13:14Z Differential interaction of antimicrobial peptides with lipid structures studied by coarse-grained molecular dynamics simulations Balatti, G.E. Ambroggio, E.E. Fidelio, G.D. Martini, M.F. Pickholz, M. Aurein Coarse-grain Helicoidal peptides Lipid bilayers Maculatin Molecular dynamics 1-palmitoyl-2-oleoylphosphatidylcholine amphibian protein antimicrobial cationic peptide aurein 1.2 peptide maculatin-1.1 protein, Litoria phosphatidylcholine chemistry computer simulation conformation lipid bilayer metabolism molecular dynamics molecular model Amphibian Proteins Antimicrobial Cationic Peptides Computer Simulation Lipid Bilayers Models, Molecular Molecular Conformation Molecular Dynamics Simulation Phosphatidylcholines 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. © 2017 by the authors. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_14203049_v22_n10_p_Balatti
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Aurein Coarse-grain Helicoidal peptides Lipid bilayers Maculatin Molecular dynamics 1-palmitoyl-2-oleoylphosphatidylcholine amphibian protein antimicrobial cationic peptide aurein 1.2 peptide maculatin-1.1 protein, Litoria phosphatidylcholine chemistry computer simulation conformation lipid bilayer metabolism molecular dynamics molecular model Amphibian Proteins Antimicrobial Cationic Peptides Computer Simulation Lipid Bilayers Models, Molecular Molecular Conformation Molecular Dynamics Simulation Phosphatidylcholines
spellingShingle	Aurein Coarse-grain Helicoidal peptides Lipid bilayers Maculatin Molecular dynamics 1-palmitoyl-2-oleoylphosphatidylcholine amphibian protein antimicrobial cationic peptide aurein 1.2 peptide maculatin-1.1 protein, Litoria phosphatidylcholine chemistry computer simulation conformation lipid bilayer metabolism molecular dynamics molecular model Amphibian Proteins Antimicrobial Cationic Peptides Computer Simulation Lipid Bilayers Models, Molecular Molecular Conformation Molecular Dynamics Simulation Phosphatidylcholines 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
topic_facet	Aurein Coarse-grain Helicoidal peptides Lipid bilayers Maculatin Molecular dynamics 1-palmitoyl-2-oleoylphosphatidylcholine amphibian protein antimicrobial cationic peptide aurein 1.2 peptide maculatin-1.1 protein, Litoria phosphatidylcholine chemistry computer simulation conformation lipid bilayer metabolism molecular dynamics molecular model Amphibian Proteins Antimicrobial Cationic Peptides Computer Simulation Lipid Bilayers Models, Molecular Molecular Conformation Molecular Dynamics Simulation Phosphatidylcholines
description	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. © 2017 by the authors.
format	JOUR
author	Balatti, G.E. Ambroggio, E.E. Fidelio, G.D. Martini, M.F. Pickholz, M.
author_facet	Balatti, G.E. Ambroggio, E.E. Fidelio, G.D. Martini, M.F. Pickholz, M.
author_sort	Balatti, G.E.
title	Differential interaction of antimicrobial peptides with lipid structures studied by coarse-grained molecular dynamics simulations
title_short	Differential interaction of antimicrobial peptides with lipid structures studied by coarse-grained molecular dynamics simulations
title_full	Differential interaction of antimicrobial peptides with lipid structures studied by coarse-grained molecular dynamics simulations
title_fullStr	Differential interaction of antimicrobial peptides with lipid structures studied by coarse-grained molecular dynamics simulations
title_full_unstemmed	Differential interaction of antimicrobial peptides with lipid structures studied by coarse-grained molecular dynamics simulations
title_sort	differential interaction of antimicrobial peptides with lipid structures studied by coarse-grained molecular dynamics simulations
url	http://hdl.handle.net/20.500.12110/paper_14203049_v22_n10_p_Balatti
work_keys_str_mv	AT balattige differentialinteractionofantimicrobialpeptideswithlipidstructuresstudiedbycoarsegrainedmoleculardynamicssimulations AT ambroggioee differentialinteractionofantimicrobialpeptideswithlipidstructuresstudiedbycoarsegrainedmoleculardynamicssimulations AT fideliogd differentialinteractionofantimicrobialpeptideswithlipidstructuresstudiedbycoarsegrainedmoleculardynamicssimulations AT martinimf differentialinteractionofantimicrobialpeptideswithlipidstructuresstudiedbycoarsegrainedmoleculardynamicssimulations AT pickholzm differentialinteractionofantimicrobialpeptideswithlipidstructuresstudiedbycoarsegrainedmoleculardynamicssimulations
_version_	1807315150523334656

Differential interaction of antimicrobial peptides with lipid structures studied by coarse-grained molecular dynamics simulations

Ejemplares similares