Study of the antimicrobial peptide indolicidin and mutants in eukaryotic modelled membrane by molecular dynamics simulations |
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Authors: | Carlos Alessandro Fuzo Léo Degrève |
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Institution: | 1. Grupo de Simula??o Molecular, Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeir?o Preto , Universidade de S?o Paulo , 14040-901, Ribeir?o Preto, S?o Paulo, Brazil cafuzo@usp.br;3. Grupo de Simula??o Molecular, Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeir?o Preto , Universidade de S?o Paulo , 14040-901, Ribeir?o Preto, S?o Paulo, Brazil |
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Abstract: | In this work the interaction of the antimicrobial peptide indolicidin (IND) and its mutants CP10A and CP11 with a eukaryotic membrane model was examined by molecular dynamics simulations. The aim was to analyse the behaviour of these antimicrobial peptides when they interact with a eukaryotic modelled membrane, thereby obtaining atomic detailed observations that are not experimentally available. In the simulations, the widely studied dipalmitoylphosphatidylcholine hydrated bilayer was used as a eukaryotic membrane model. In agreement with experimental observations, the peptides IND, CP10A, and CP11 insert into the bilayer differently; the peptides that insert more deeply present the major hemolytic activities. The hydrophobic residues are responsible for the insertion, but some Trp residues of the peptides remain at the bilayer/water interface because they interact with the bilayer choline groups by cation-π interactions that should be important for recognition of eukaryotic membrane by the three studied peptides. |
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Keywords: | antimicrobial peptide indolicidin peptide-membrane interaction cation-π interaction molecular dynamics simulation |
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