ArticleBiophysical journal2008
Temperature-induced dissociation of Abeta monomers from amyloid fibril.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- On the reversibility of amyloid fibril formation.Biophysics reviews · 2025Review
- Survey of the Aβ-peptide structural diversity: molecular dynamics approaches.Biophysical reviews · 2024Review
- Deciphering the Disaggregation Mechanism of Amyloid Beta Aggregate by 4-(2-Hydroxyethyl)-1-Piperazinepropanesulfonic Acid Using Electrochemical Impedance Spectroscopy.Sensors (Basel, Switzerland) · 2021Article
- Atomic Force Microscopy Analysis of EPPS-Driven Degradation and Reformation of Amyloid-β Aggregates.Journal of Alzheimer's disease reports · 2018Article
- A brief overview of amyloids and Alzheimer's disease.Protein science : a publication of the Protein Society · 2014Review
- Side-chain hydrophobicity and the stability of Aβ₁₆₋₂₂ aggregates.Protein science : a publication of the Protein Society · 2012Article
- Structure and dynamics of amyloid-β segmental polymorphisms.PloS one · 2012Article
- Amyloid features and neuronal toxicity of mature prion fibrils are highly sensitive to high pressure.The Journal of biological chemistry · 2011Article
- Computational backbone mutagenesis of Abeta peptides: probing the role of backbone hydrogen bonds in aggregation.The journal of physical chemistry. B · 2010Article
- Association thermodynamics and conformational stability of beta-sheet amyloid beta(17-42) oligomers: effects of E22Q (Dutch) mutation and charge neutralization.Biophysical journal · 2010Article
- Interpeptide interactions induce helix to strand structural transition in Abeta peptides.Proteins · 2009Article
- Side chain interactions can impede amyloid fibril growth: replica exchange simulations of Abeta peptide mutant.The journal of physical chemistry. B · 2009Article
- Probing energetics of Abeta fibril elongation by molecular dynamics simulations.Biophysical journal · 2009Article
- Replica exchange simulations of the thermodynamics of Abeta fibril growth.Biophysical journal · 2009Article
- The binding of thioflavin T and its neutral analog BTA-1 to protofibrils of the Alzheimer's disease Abeta(16-22) peptide probed by molecular dynamics simulations.Journal of molecular biology · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Using all-atom molecular dynamics, we study the temperature-induced dissociation of Abeta monomers from the fibril protofilament. To accelerate conformational sampling, simulations are performed at elevated temperatures and peptide concentrations. By computing free energy disconnectivity graphs we mapped the free energy landscape of monomers on the surface of Abeta fibril. We found that Abeta monomers sample diverse sets of low free energy states with different degrees of association with the fibril. Some of these states have residual amounts of fibril interactions, whereas others lack fibril-like content. Generally, Abeta monomers with partially formed fibril-like interactions have the lowest free energies, but their backbone conformations may differ considerably from those in the fibril interior. Overall, Abeta amyloid protofilaments seem to be highly resistant to thermal dissociation. Monomer dissociation from the fibril edge proceeds via multiple stages and pathways. Our simulation findings are discussed in the context of recent experimental results.
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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.