ArticleProceedings of the National Academy of Sciences of the United States of America2020
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Engineering Nanotherapeutics Through Interfacial Mechanics: Mechanobiology and Precision Drug Delivery.Micromachines · 2026Article
- Quantitative Analysis of Amyloid Fibril Nucleation by Linking Folding and Nucleation Pathways Using a Robust Ultrasonic Assay.ACS omega · 2026Article
- Modeling Protein Aggregation Kinetics from NMR Data.Journal of molecular biology · 2025Review
- General integrated rate law for complex self-assembly reactions reveals the mechanism of amyloid-beta coaggregation.Physical chemistry chemical physics : PCCP · 2025Article
- Mechanism of inhibition of acid-mediated transthyretin aggregation by designed peptides.The Journal of biological chemistry · 2025Article
- Direct Observation of Secondary Nucleation in Huntingtin Amyloid Formation by High-Speed Atomic Force Microscopy.Journal of the American Chemical Society · 2025Article
- Inhibitor-based modulation of huntingtin aggregation mechanisms mitigates fibril-induced cellular stress.Nature communications · 2025Article
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- Review
- Aggregation of the amyloid-β peptide (Aβ40) within condensates generated through liquid-liquid phase separation.Scientific reports · 2024Article
- Heterotypic Seeding Generates Mixed Amyloid Polymorphs.Small science · 2024Article
- O-GlcNAc Modification of α-Synuclein Can Alter Monomer Dynamics to Control Aggregation Kinetics.ACS chemical neuroscience · 2024Article
- Kinetic models reveal the interplay of protein production and aggregation.Chemical science · 2024Article
- Pharmacological inhibition of α-synuclein aggregation within liquid condensates.Nature communications · 2024Article
- Exploration of Resveratrol as a Potent Modulator of α-Synuclein Fibril Formation.ACS chemical neuroscience · 2024Article
- Photocontrol of the β-Hairpin Polypeptide Structure through an Optimized Azobenzene-Based Amino Acid Analogue.Journal of the American Chemical Society · 2024Article
- Differential Effects of Lipid Bilayers on αPSM Peptide Functional Amyloid Formation.International journal of molecular sciences · 2023Article
- Influence of Amino Acid Substitutions in ApoMb on Different Stages of Unfolding of Amyloids.Molecules (Basel, Switzerland) · 2023Article
- Secondary Processes Dominate the Quiescent, Spontaneous Aggregation of α-Synuclein at Physiological pH with Sodium Salts.ACS chemical neuroscience · 2023Article
- Decoding the Roles of Amyloid-β (1-42)'s Key Oligomerization Domains toward Designing Epitope-Specific Aggregation Inhibitors.JACS Au · 2023Article
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Authors and funding
10 authors.
Funding
Abstract
Understanding the mechanism of action of compounds capable of inhibiting amyloid-fibril formation is critical to the development of potential therapeutics against protein-misfolding diseases. A fundamental challenge for progress is the range of possible target species and the disparate timescales involved, since the aggregating proteins are simultaneously the reactants, products, intermediates, and catalysts of the reaction. It is a complex problem, therefore, to choose the states of the aggregating proteins that should be bound by the compounds to achieve the most potent inhibition. We present here a comprehensive kinetic theory of amyloid-aggregation inhibition that reveals the fundamental thermodynamic and kinetic signatures characterizing effective inhibitors by identifying quantitative relationships between the aggregation and binding rate constants. These results provide general physical laws to guide the design and optimization of inhibitors of amyloid-fibril formation, revealing in particular the important role of on-rates in the binding of the inhibitors.
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