ArticleACS chemical neuroscience2014
The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length.
Article in ACS chemical neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Molecular Dynamics Simulations of 4Computational and structural biotechnology journal · 2026Article
- Molecular Characterization of the GALC Mutation Thr112Ala Causing Krabbe Disease.International journal of molecular sciences · 2025Article
- Mutations in the B.1.1.7 SARS-CoV-2 Spike Protein Reduce Receptor-Binding Affinity and Induce a Flexible Link to the Fusion Peptide.Biomedicines · 2021Article
- Molecular interactions between monoclonal oligomer-specific antibody 5E3 and its amyloid beta cognates.PloS one · 2020Article
- Alkali ion influence on structure and stability of fibrillar amyloid-β oligomers.Journal of molecular modeling · 2019Article
- Role of the N-terminus for the stability of an amyloid-β fibril with three-fold symmetry.PloS one · 2017Article
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Authors and funding
3 authors.
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Abstract
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 attributed to an extension of the middle strand of a three-stranded antiparallel β sheet through residues 41-43, only present in the longer Aβ species that aggregate faster and are more neurotoxic. Additional MD simulations demonstrate that this higher stability is also present in the monomers forming the tetramer. In conclusion, our findings suggest the existence of a nonfibrillar oligomer topology that is significantly more stable for the longer Aβ species, thus offering a structural explanation for their higher neurotoxicity.
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