A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures

In the present work we investigated the differential interactions of the antimicrobial peptides (AMPs) aurein 1.2 and maculatin 1.1 with a bilayer composed of a mixture of the lipids 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (POPG) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethan...

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Autores principales:	Balatti, G.E., Martini, M.F., Pickholz, M.
Formato:	JOUR
Materias:	Antimicrobial peptides Aurein Coarse-grained Maculatin Molecular dynamics 1 palmitoyl 2 oleoyl sn glycero 3 phospho (1' rac glycerol) 1 palmitoyl 2 oleoyl sn glycero 3 phosphoethanolamine 2 oleoyl 1 palmitoylphosphatidylcholine aurein 1.2 lipid maculatin 1.1 polypeptide antibiotic agent unclassified drug water 1-palmitoyl-2-oleoylglycero-3-phosphoglycerol 1-palmitoyl-2-oleoylphosphatidylcholine 1-palmitoyl-2-oleoylphosphatidylethanolamine amphibian protein antiinfective agent antimicrobial cationic peptide aurein 1.2 peptide maculatin-1.1 protein, Litoria phosphatidylcholine phosphatidylethanolamine phosphatidylglycerol protein binding Article bacterial membrane drug mixture lipid bilayer molecular dynamics priority journal prokaryotic cell protein lipid interaction alpha helix amino acid sequence animal Anura binding site chemical phenomena chemistry isolation and purification metabolism protein domain Amino Acid Sequence Amphibian Proteins Animals Anti-Bacterial Agents Antimicrobial Cationic Peptides Binding Sites Hydrophobic and Hydrophilic Interactions Lipid Bilayers Molecular Dynamics Simulation Phosphatidylcholines Phosphatidylethanolamines Phosphatidylglycerols Protein Binding Protein Conformation, alpha-Helical Protein Interaction Domains and Motifs
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_16102940_v24_n8_p_Balatti
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	todo:paper_16102940_v24_n8_p_Balatti2023-10-03T16:27:55Z A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures Balatti, G.E. Martini, M.F. Pickholz, M. Antimicrobial peptides Aurein Coarse-grained Maculatin Molecular dynamics 1 palmitoyl 2 oleoyl sn glycero 3 phospho (1' rac glycerol) 1 palmitoyl 2 oleoyl sn glycero 3 phosphoethanolamine 2 oleoyl 1 palmitoylphosphatidylcholine aurein 1.2 lipid maculatin 1.1 polypeptide antibiotic agent unclassified drug water 1-palmitoyl-2-oleoylglycero-3-phosphoglycerol 1-palmitoyl-2-oleoylphosphatidylcholine 1-palmitoyl-2-oleoylphosphatidylethanolamine amphibian protein antiinfective agent antimicrobial cationic peptide aurein 1.2 peptide maculatin-1.1 protein, Litoria phosphatidylcholine phosphatidylethanolamine phosphatidylglycerol protein binding Article bacterial membrane drug mixture lipid bilayer molecular dynamics priority journal prokaryotic cell protein lipid interaction alpha helix amino acid sequence animal Anura binding site chemical phenomena chemistry isolation and purification lipid bilayer metabolism protein domain Amino Acid Sequence Amphibian Proteins Animals Anti-Bacterial Agents Antimicrobial Cationic Peptides Anura Binding Sites Hydrophobic and Hydrophilic Interactions Lipid Bilayers Molecular Dynamics Simulation Phosphatidylcholines Phosphatidylethanolamines Phosphatidylglycerols Protein Binding Protein Conformation, alpha-Helical Protein Interaction Domains and Motifs In the present work we investigated the differential interactions of the antimicrobial peptides (AMPs) aurein 1.2 and maculatin 1.1 with a bilayer composed of a mixture of the lipids 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (POPG) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE). We carried out molecular dynamics (MD) simulations using a coarse-grained approach within the MARTINI force field. The POPE/POPG mixture was used as a simple model of a bacterial (prokaryotic cell) membrane. The results were compared with our previous findings for structures of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), a representative lipid of mammalian cells. We started the simulations of the peptide–lipid system from two different initial conditions: peptides in water and peptides inside the hydrophobic core of the membrane, employing a pre-assembled lipid bilayer in both cases. Our results show similarities and differences regarding the molecular behavior of the peptides in POPE/POPG in comparison to their behavior in a POPC membrane. For instance, aurein 1.2 molecules can adopt similar pore-like structures on both POPG/POPE and POPC membranes, but the peptides are found deeper in the hydrophobic core in the former. Maculatin 1.1 molecules, in turn, achieve very similar structures in both kinds of bilayers: they have a strong tendency to form clusters and induce curvature. Therefore, the results of this study provide insight into the mechanisms of action of these two peptides in membrane leakage, which allows organisms to protect themselves against potentially harmful bacteria. [Figure not available: see fulltext.]. © 2018, Springer-Verlag GmbH Germany, part of Springer Nature. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_16102940_v24_n8_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	Antimicrobial peptides Aurein Coarse-grained Maculatin Molecular dynamics 1 palmitoyl 2 oleoyl sn glycero 3 phospho (1' rac glycerol) 1 palmitoyl 2 oleoyl sn glycero 3 phosphoethanolamine 2 oleoyl 1 palmitoylphosphatidylcholine aurein 1.2 lipid maculatin 1.1 polypeptide antibiotic agent unclassified drug water 1-palmitoyl-2-oleoylglycero-3-phosphoglycerol 1-palmitoyl-2-oleoylphosphatidylcholine 1-palmitoyl-2-oleoylphosphatidylethanolamine amphibian protein antiinfective agent antimicrobial cationic peptide aurein 1.2 peptide maculatin-1.1 protein, Litoria phosphatidylcholine phosphatidylethanolamine phosphatidylglycerol protein binding Article bacterial membrane drug mixture lipid bilayer molecular dynamics priority journal prokaryotic cell protein lipid interaction alpha helix amino acid sequence animal Anura binding site chemical phenomena chemistry isolation and purification lipid bilayer metabolism protein domain Amino Acid Sequence Amphibian Proteins Animals Anti-Bacterial Agents Antimicrobial Cationic Peptides Anura Binding Sites Hydrophobic and Hydrophilic Interactions Lipid Bilayers Molecular Dynamics Simulation Phosphatidylcholines Phosphatidylethanolamines Phosphatidylglycerols Protein Binding Protein Conformation, alpha-Helical Protein Interaction Domains and Motifs
spellingShingle	Antimicrobial peptides Aurein Coarse-grained Maculatin Molecular dynamics 1 palmitoyl 2 oleoyl sn glycero 3 phospho (1' rac glycerol) 1 palmitoyl 2 oleoyl sn glycero 3 phosphoethanolamine 2 oleoyl 1 palmitoylphosphatidylcholine aurein 1.2 lipid maculatin 1.1 polypeptide antibiotic agent unclassified drug water 1-palmitoyl-2-oleoylglycero-3-phosphoglycerol 1-palmitoyl-2-oleoylphosphatidylcholine 1-palmitoyl-2-oleoylphosphatidylethanolamine amphibian protein antiinfective agent antimicrobial cationic peptide aurein 1.2 peptide maculatin-1.1 protein, Litoria phosphatidylcholine phosphatidylethanolamine phosphatidylglycerol protein binding Article bacterial membrane drug mixture lipid bilayer molecular dynamics priority journal prokaryotic cell protein lipid interaction alpha helix amino acid sequence animal Anura binding site chemical phenomena chemistry isolation and purification lipid bilayer metabolism protein domain Amino Acid Sequence Amphibian Proteins Animals Anti-Bacterial Agents Antimicrobial Cationic Peptides Anura Binding Sites Hydrophobic and Hydrophilic Interactions Lipid Bilayers Molecular Dynamics Simulation Phosphatidylcholines Phosphatidylethanolamines Phosphatidylglycerols Protein Binding Protein Conformation, alpha-Helical Protein Interaction Domains and Motifs Balatti, G.E. Martini, M.F. Pickholz, M. A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures
topic_facet	Antimicrobial peptides Aurein Coarse-grained Maculatin Molecular dynamics 1 palmitoyl 2 oleoyl sn glycero 3 phospho (1' rac glycerol) 1 palmitoyl 2 oleoyl sn glycero 3 phosphoethanolamine 2 oleoyl 1 palmitoylphosphatidylcholine aurein 1.2 lipid maculatin 1.1 polypeptide antibiotic agent unclassified drug water 1-palmitoyl-2-oleoylglycero-3-phosphoglycerol 1-palmitoyl-2-oleoylphosphatidylcholine 1-palmitoyl-2-oleoylphosphatidylethanolamine amphibian protein antiinfective agent antimicrobial cationic peptide aurein 1.2 peptide maculatin-1.1 protein, Litoria phosphatidylcholine phosphatidylethanolamine phosphatidylglycerol protein binding Article bacterial membrane drug mixture lipid bilayer molecular dynamics priority journal prokaryotic cell protein lipid interaction alpha helix amino acid sequence animal Anura binding site chemical phenomena chemistry isolation and purification lipid bilayer metabolism protein domain Amino Acid Sequence Amphibian Proteins Animals Anti-Bacterial Agents Antimicrobial Cationic Peptides Anura Binding Sites Hydrophobic and Hydrophilic Interactions Lipid Bilayers Molecular Dynamics Simulation Phosphatidylcholines Phosphatidylethanolamines Phosphatidylglycerols Protein Binding Protein Conformation, alpha-Helical Protein Interaction Domains and Motifs
description	In the present work we investigated the differential interactions of the antimicrobial peptides (AMPs) aurein 1.2 and maculatin 1.1 with a bilayer composed of a mixture of the lipids 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (POPG) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE). We carried out molecular dynamics (MD) simulations using a coarse-grained approach within the MARTINI force field. The POPE/POPG mixture was used as a simple model of a bacterial (prokaryotic cell) membrane. The results were compared with our previous findings for structures of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), a representative lipid of mammalian cells. We started the simulations of the peptide–lipid system from two different initial conditions: peptides in water and peptides inside the hydrophobic core of the membrane, employing a pre-assembled lipid bilayer in both cases. Our results show similarities and differences regarding the molecular behavior of the peptides in POPE/POPG in comparison to their behavior in a POPC membrane. For instance, aurein 1.2 molecules can adopt similar pore-like structures on both POPG/POPE and POPC membranes, but the peptides are found deeper in the hydrophobic core in the former. Maculatin 1.1 molecules, in turn, achieve very similar structures in both kinds of bilayers: they have a strong tendency to form clusters and induce curvature. Therefore, the results of this study provide insight into the mechanisms of action of these two peptides in membrane leakage, which allows organisms to protect themselves against potentially harmful bacteria. [Figure not available: see fulltext.]. © 2018, Springer-Verlag GmbH Germany, part of Springer Nature.
format	JOUR
author	Balatti, G.E. Martini, M.F. Pickholz, M.
author_facet	Balatti, G.E. Martini, M.F. Pickholz, M.
author_sort	Balatti, G.E.
title	A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures
title_short	A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures
title_full	A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures
title_fullStr	A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures
title_full_unstemmed	A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures
title_sort	coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with popg/pope lipid mixtures
url	http://hdl.handle.net/20.500.12110/paper_16102940_v24_n8_p_Balatti
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A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures

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