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• W2032903886 endingPage "52" @default.
• W2032903886 startingPage "44" @default.
• W2032903886 abstract "The amyloid β-peptide (Aβ) is a 40-42 residue peptide that is the principal toxic species in Alzheimer's disease (AD). The oxidation of methionine-35 (Met35) to the sulfoxide form (Met35(ox)) has been identified as potential modulator of Aβ aggregation. The role Met35(ox) plays in Aβ neurotoxicity differs among experimental studies, which may be due to inconsistent solution conditions (pH, buffer, temperature). We applied atomistic molecular dynamics (MD) simulations as a means to probe the dynamics of the monomeric 40-residue alloform of Aβ (Aβ40) containing Met35 or Met35(ox) in an effort to resolve the conflicting experimental results. We found that Met35 oxidation decreases the β-strand content of the C-terminal hydrophobic region (residues 29-40), with a specific effect on the secondary structure of residues 33-35, thus potentially impeding aggregation. Further, there is an important interplay between oxidation state and solution conditions, with pH and salt concentration augmenting the effects of oxidation. The results presented here serve to rationalize the conflicting results seen in experimental studies and provide a fundamental biophysical characterization of monomeric Aβ40 dynamics in both reduced and oxidized forms, providing insight into the biochemical mechanism of Aβ40 and oxidative stress related to AD." @default.
• W2032903886 created "2016-06-24" @default.
• W2032903886 creator A5025714037 @default.
• W2032903886 creator A5046097854 @default.
• W2032903886 creator A5049055647 @default.
• W2032903886 creator A5081565182 @default.
• W2032903886 date "2014-03-01" @default.
• W2032903886 modified "2023-09-30" @default.
• W2032903886 title "Simulations of monomeric amyloid β-peptide (1–40) with varying solution conditions and oxidation state of Met35: Implications for aggregation" @default.
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• W2032903886 doi "https://doi.org/10.1016/j.abb.2014.01.002" @default.
• W2032903886 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24418316" @default.
• W2032903886 hasPublicationYear "2014" @default.
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