ArticleJournal of the American Chemical Society2013
Polymorph-specific kinetics and thermodynamics of β-amyloid fibril growth.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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Who cites it
89 citing papers in PubMed, 158 citations in OpenAlex.
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- Structural Basis of Amyloid Fibril Assembly by Plant Seed Storage Proteins.Nature communications · 2026Article
- Amyloid fibril polymorphism: Structural mechanisms of assembly and the links to disease.Current opinion in structural biology · 2026Review
- Exploring the Impact of Curcumin and Carbon Nanotubes on Beta-amyloid Peptide Dimer: Insights from Molecular Dynamics Simulation and Density Functional Theory Methods.Current pharmaceutical biotechnology · 2026Article
- Time-resolved solid-state nuclear magnetic resonance studies of amyloid-β oligomer formation.Methods in enzymology · 2026Review
- Single-fibril Förster resonance energy transfer imaging and deep learning reveal concentration dependence of amyloid β 42 aggregation pathways.PNAS nexus · 2025Article
- Chameleonic Nature of Aβ: Implications for Alzheimer's and Other Amyloid Diseases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Low-frequency Raman spectra of amyloid fibrils.The Journal of chemical physics · 2025Article
- Generating the polymorph landscapes of amyloid fibrils using AI: RibbonFold.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- On the reversibility of amyloid fibril formation.Biophysics reviews · 2025Review
- Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024Review
- Principles and Biomedical Applications of Self-Assembled Peptides: Potential Treatment of Type 2 Diabetes Mellitus.Pharmaceutics · 2024Review
- The role of shear forces in primary and secondary nucleation of amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Rigidifying of the internal dynamics of amyloid-beta fibrils generated in the presence of synaptic plasma vesicles.Physical chemistry chemical physics : PCCP · 2024Article
- Simultaneously Measured Kinetics of Two Amyloid Polymorphs Using Cross Peak Specific 2D IR Spectroscopy.The journal of physical chemistry letters · 2023Article
- Article
- Nucleation and Growth of Amyloid Fibrils.The journal of physical chemistry. B · 2023Article
- Amyloid fibril structures of tau: Conformational plasticity of the second microtubule-binding repeat.Science advances · 2023Article
- Early events in amyloid-β self-assembly probed by time-resolved solid state NMR and light scattering.Nature communications · 2023Article
- Liquid Droplet Aging and Seeded Fibril Formation of the Cytotoxic Granule Associated RNA Binding Protein TIA1 Low Complexity Domain.Journal of the American Chemical Society · 2023Article
29 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Amyloid fibrils formed by the 40-residue β-amyloid peptide (Aβ(1-40)) are highly polymorphic, with molecular structures that depend on the details of growth conditions. Underlying differences in physical properties are not well understood. Here, we investigate differences in growth kinetics and thermodynamic stabilities of two Aβ(1-40) fibril polymorphs for which detailed structural models are available from solid-state nuclear magnetic resonance (NMR) studies. Rates of seeded fibril elongation in the presence of excess soluble Aβ(1-40) and shrinkage in the absence of soluble Aβ(1-40) are determined with atomic force microscopy (AFM). From these rates, we derive polymorph-specific values for the soluble Aβ(1-40) concentration at quasi-equilibrium, from which relative stabilities can be derived. The AFM results are supported by direct measurements by ultraviolet absorbance, using a novel dialysis system to establish quasi-equilibrium. At 24 °C, the two polymorphs have significantly different elongation and shrinkage kinetics but similar thermodynamic stabilities. At 37 °C, differences in kinetics are reduced, and thermodynamic stabilities are increased significantly. Fibril length distributions in AFM images provide support for an intermittent growth model, in which fibrils switch randomly between an "on" state (capable of elongation) and an "off" state (incapable of elongation). We also monitor interconversion between polymorphs at 24 °C by solid-state NMR, showing that the two-fold symmetric "agitated" (A) polymorph is more stable than the three-fold symmetric "quiescent" (Q) polymorph. Finally, we show that the two polymorphs have significantly different rates of fragmentation in the presence of shear forces, a difference that helps explain the observed predominance of the A structure when fibrils are grown in agitated solutions.
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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.