ArticleThe journal of physical chemistry. B2009
Side chain interactions can impede amyloid fibril growth: replica exchange simulations of Abeta peptide mutant.
Article in The journal of physical chemistry. B, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.International journal of molecular sciences · 2018Review
- Oligomerization of FVFLM peptides and their ability to inhibit beta amyloid peptides aggregation: consideration as a possible model.Physical chemistry chemical physics : PCCP · 2017Article
- Is the Conformational Ensemble of Alzheimer's Aβ10-40 Peptide Force Field Dependent?PLoS computational biology · 2017Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Article
- Conformational stability of fibrillar amyloid-beta oligomers via protofilament pair formation - a systematic computational study.PloS one · 2013Article
- Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Cold Spring Harbor perspectives in medicine · 2012Review
- Toward a molecular theory of early and late events in monomer to amyloid fibril formation.Annual review of physical chemistry · 2011Review
- Mapping conformational ensembles of aβ oligomers in molecular dynamics simulations.Biophysical journal · 2010Article
- Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Chemical reviews · 2010Review
- Globular state in the oligomers formed by Abeta peptides.The Journal of chemical physics · 2010Article
- Computational backbone mutagenesis of Abeta peptides: probing the role of backbone hydrogen bonds in aggregation.The journal of physical chemistry. B · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Using replica exchange molecular dynamics, we study the effect of Asp23Tyr mutation on Abeta(10-40) fibril growth. The effect of this mutation is revealed through the computation of free energy landscapes, the distributions of peptide-fibril interactions, and by comparison with the wild-type Abeta(10-40) peptide. Asp23Tyr mutation has a relatively minor influence on the docking of Abeta peptides to the fibril. However, it has a strong impact on the locking stage due to profound stabilization of the parallel in-registry beta-sheets formed by the peptides on the fibril edge. The enhanced stability of parallel beta-sheets results from the deletion of side chain interactions formed by Asp23, which are incompatible with the fibril-like conformers. Consequently, Asp23Tyr mutation is expected to promote fibril growth. We argue that strong off-registry side chain interactions may slow down fibril assembly as it occurs for the wild-type Abeta peptide. The analysis of experimental data offers support to our in silico conclusions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.