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...

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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

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