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- W2970060356 abstract "We performed coarse-grained computer simulations using MARTINI force field to study the difference in the self-assembly and possible pore creation in DPPC phospholipid membranes by two different antimicrobial peptides: magainin-2 and melittin. Simulations showed that magainin-2 peptides create large sized disordered toroidal pores that allow easy water permeation across them. Melittin assemblies contain peptides in U-shaped conformations that, although creating holes in membranes, block effectively the passage of water. These observed structures are consistent with the dye efflux experiments performed on vesicles exposed to solutions containing antimicrobial peptides." @default.
- W2970060356 created "2019-09-05" @default.
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- W2970060356 date "2012-01-01" @default.
- W2970060356 modified "2023-09-24" @default.
- W2970060356 title "Difference between Magainin-2 and Melittin Assemblies in Phosphatidylcholine Bilayers: Results from Coarse-Grained Simulations B" @default.
- W2970060356 hasPublicationYear "2012" @default.
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