The conformational stability of nonfibrillar amyloid-? peptide oligomers critically depends on the C-terminal peptide length.
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ABSTRACT:
SUBMITTER: Socher E
PROVIDER: S-EPMC3963130 | biostudies-literature | 2014 Mar
REPOSITORIES: biostudies-literature
Publications
The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length.
Socher Eileen E Sticht Heinrich H Horn Anselm H C AH
ACS chemical neuroscience 20140211 3
The amyloid-β (Aβ) peptide is one key molecule in the pathogenesis of Alzheimer's disease. We investigated the conformational stability of a nonfibrillar tetrameric Aβ structure by molecular dynamics (MD) simulations revealing that the stability of the Aβ tetramer depends critically on the C-terminal length. In contrast to the Aβ17-40 tetramer, which proved to be instable, the simulations demonstrate structural integrity of the Aβ17-42 and Aβ17-43 tetramers. These differences in stability can be ...[more]
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