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- W2092124534 abstract "Neurodegenerative pathologies such as Alzheimer's disease affect millions of people worldwide and are a major cause of morbidity and mortality. One such cause of dementia, Creutzfeld-Jakob disease, is thought to be caused by the human prion protein PrP. Interactions with membranes have been shown to affect the behaviour of amyloid-forming peptides, including prion peptides, and have been implicated in their toxicity. To gain insight into the molecular basis of these effects, we use atomistic molecular dynamics simulations in explicit solvent to examine the interaction of several blocked PrP and yeast-prion protein fragments with zwitterionic and anionic lipid bilayers. All four oligopeptide sequences are studied at different concentrations, successively in the presence of phosphatidylcholine (POPC, zwitterionic) and phosphatidylserine (POPS, anionic) bilayers, for a total of 0.12 ms of simulation time. Peptide-lipid interactions are characterized and the effect of peptide binding to the lipid bilayers on the conformational ensemble and self-aggregation properties of the peptides is analyzed. Possible implications of these findings to prion peptide toxicity are discussed." @default.
- W2092124534 created "2016-06-24" @default.
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- W2092124534 date "2011-02-01" @default.
- W2092124534 modified "2023-09-27" @default.
- W2092124534 title "Molecular Simulation Study of Prion Peptide Self-Aggregation in the Presence of Lipid Membranes" @default.
- W2092124534 doi "https://doi.org/10.1016/j.bpj.2010.12.3679" @default.
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