ArticleBiophysical journal2010
Mapping conformational ensembles of aβ oligomers in molecular dynamics simulations.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Survey of the Aβ-peptide structural diversity: molecular dynamics approaches.Biophysical reviews · 2024Review
- Peptide Solubility Limits: Backbone and Side-Chain Interactions.The journal of physical chemistry. B · 2018Article
- Initial Structural Models of the Aβ42 Dimer from Replica Exchange Molecular Dynamics Simulations.ACS omega · 2017Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Solubility and aggregation of Gly(5) in water.The journal of physical chemistry. B · 2014Article
- The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length.ACS chemical neuroscience · 2014Article
- Conformational distribution and α-helix to β-sheet transition of human amylin fragment dimer.Biomacromolecules · 2014Article
- Article
- A simple lattice model that captures protein folding, aggregation and amyloid formation.PloS one · 2014Article
- Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.Journal of molecular biology · 2013Article
- Reduced atomic pair-interaction design (RAPID) model for simulations of proteins.The Journal of chemical physics · 2013Article
- Binding to the lipid monolayer induces conformational transition in Aβ monomer.Journal of molecular modeling · 2013Article
- Stochastic simulation of structural properties of natively unfolded and denatured proteins.Journal of molecular modeling · 2012Article
- Flexibility and binding affinity in protein-ligand, protein-protein and multi-component protein interactions: limitations of current computational approaches.Journal of the Royal Society, Interface · 2012Review
- Article
- Disordered binding of small molecules to Aβ(12-28).The Journal of biological chemistry · 2011Article
- Does amino acid sequence determine the properties of Aβ dimer?The Journal of chemical physics · 2011Article
- Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.Biochemistry · 2011Article
- Naproxen interferes with the assembly of Aβ oligomers implicated in Alzheimer's disease.Biophysical journal · 2011Article
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Authors and funding
3 authors.
Funding
Abstract
Although the oligomers formed by Aβ peptides appear to be the primary cytotoxic species in Alzheimer's disease, detailed information about their structures appears to be lacking. In this article, we use exhaustive replica exchange molecular dynamics and an implicit solvent united-atom model to study the structural properties of Aβ monomers, dimers, and tetramers. Our analysis suggests that the conformational ensembles of Aβ dimers and tetramers are very similar, but sharply distinct from those sampled by the monomers. The key conformational difference between monomers and oligomers is the formation of β-structure in the oligomers occurring together with the loss of intrapeptide interactions and helix structure. Our simulations indicate that, independent of oligomer order, the Aβ aggregation interface is largely confined to the sequence region 10-23, which forms the bulk of interpeptide interactions. We show that the fractions of β structure computed in our simulations and measured experimentally are in good agreement.
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