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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Detalles Bibliográficos
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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