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- W2086379192 abstract "To gain insight into the aggregation and oligomerization of antimicrobial or amyloidogenic peptides, we carried out molecular dynamics simulations of a 26-residue amphipathic peptide at different concentrations (8, 16, and 32 copies) in a fully hydrated bilayer composed of 1600 POPC lipid molecules. With a coarse-grained representation of the molecules, >28 microseconds of simulations were accumulated for each system. Oligomers of various orders were observed to form. The system with 32 copies of the peptide was finally comprised of a 4-, 7-, 8-, and 13-mer. The final compositions of the systems with 16 and 8 copies of the peptide were 3-, 4-, and 9-mer for one and 3- and 5-mer for the other. Higher oligomers were formed by addition of monomers and by association of pre-formed lower oligomers (see Figure). Dissociation was not observed. In the lower oligomers (up to 4-mer) only the hydrophilic side of each copy was buried, but in the higer oligomers the hydrophobic sides of some copies were also buried. These simulations provide molecular insight into oligomerization of peptides inside membranes." @default.
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- W2086379192 date "2010-01-01" @default.
- W2086379192 modified "2023-10-14" @default.
- W2086379192 title "Oligomerization of Amphipathic Peptides in a Membrane Studied by Coarse-Grained Molecular Dynamics Simulations" @default.
- W2086379192 doi "https://doi.org/10.1016/j.bpj.2009.12.2489" @default.
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