ArticlePLoS computational biology2020
The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth.
Article in PLoS computational biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Structure of Water in the First Hydration Shell of the Highly Hydrophobic Anthracene.The journal of physical chemistry. A · 2026Article
- Bioinformatic assessment of the potential amyloidogenicity of the human and evolutionarily more ancient proteomes.The Biochemical journal · 2026Article
- The temperature dependence of amyloidProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development.Matrix biology : journal of the International Society for Matrix Biology · 2026Article
- Thermodynamic stability modulates chaperone-mediated disaggregation of α-synuclein fibrils.Chemical science · 2026Article
- PLM-eXplain: divide and conquer the protein embedding space.Bioinformatics (Oxford, England) · 2026Article
- The Influence of POPC as a Coaggregate in Amyloid-β Oligomer Formation.ACS chemical neuroscience · 2025Article
- Structural flexibility in the ordered domain of the dengue virus strain 2 capsid protein is critical for chaperoning viral RNA replication.Cellular and molecular life sciences : CMLS · 2025Article
- Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation.Journal of advanced research · 2025Review
- Inhibition of Aβ Aggregation by Cholesterol-End-Modified PEG Vesicles and Micelles.Pharmaceutics · 2024Article
- AlzDiscovery: A computational tool to identify Alzheimer's disease-causing missense mutations using protein structure information.Protein science : a publication of the Protein Society · 2024Article
- Raman Spectroscopic Insights of Phase-Separated Insulin Aggregates.ACS physical chemistry Au · 2024Article
- Structure-Toxicity Relationship in Intermediate Fibrils from α-Synuclein Condensates.Journal of the American Chemical Society · 2024Article
- Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation.Chemical science · 2024Article
- Martini on the Rocks: Can a Coarse-Grained Force Field Model Crystals?The journal of physical chemistry letters · 2024Article
- Solvation thermodynamics from cavity shapes of amino acids.PNAS nexus · 2023Article
- Molecular Design of Magnetic Resonance Imaging Agents Binding to Amyloid Deposits.International journal of molecular sciences · 2023Review
- Simulations of Amyloid-Forming Peptides in the Crystal State.The protein journal · 2023Article
- Aggregation of Amyloidogenic Peptide Uperin-Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2023Article
- Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models.International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many proteins have the potential to aggregate into amyloid fibrils, protein polymers associated with a wide range of human disorders such as Alzheimer's and Parkinson's disease. The thermodynamic stability of amyloid fibrils, in contrast to that of folded proteins, is not well understood: the balance between entropic and enthalpic terms, including the chain entropy and the hydrophobic effect, are poorly characterised. Using a combination of theory, in vitro experiments, simulations of a coarse-grained protein model and meta-data analysis, we delineate the enthalpic and entropic contributions that dominate amyloid fibril elongation. Our prediction of a characteristic temperature-dependent enthalpic signature is confirmed by the performed calorimetric experiments and a meta-analysis over published data. From these results we are able to define the necessary conditions to observe cold denaturation of amyloid fibrils. Overall, we show that amyloid fibril elongation is associated with a negative heat capacity, the magnitude of which correlates closely with the hydrophobic surface area that is buried upon fibril formation, highlighting the importance of hydrophobicity for fibril stability.
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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.