ArticleProceedings of the National Academy of Sciences of the United States of America2022
Adsorption free energy predicts amyloid protein nucleation rates.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Data-driven pipeline enables discovery of plant protein surfactants.Communications chemistry · 2026Article
- Inhibition and Formation of Amyloid Fibrils in the Bulk and at the Interface of Biomolecular Condensates.Angewandte Chemie (International ed. in English) · 2026Review
- Collective Variable-Guided Engineering of the Free-Energy Surface of a Small Peptide.Journal of chemical information and modeling · 2026Article
- Structural defects in amyloid-β fibrils drive secondary nucleation.Nature communications · 2026Article
- Article
- Nanoscale Analysis beyond Imaging by Atomic Force Microscopy: Molecular Perspectives on Oncology and Neurodegeneration.Small science · 2025Review
- General integrated rate law for complex self-assembly reactions reveals the mechanism of amyloid-beta coaggregation.Physical chemistry chemical physics : PCCP · 2025Article
- Article
- Aβ42 promotes the aggregation of α-synuclein splice isoforms via heterogeneous nucleation.FEBS letters · 2025Article
- Recruitment of Aβ into α‑Synuclein Condensates Catalyzes Primary Nucleation of α‑Synuclein Aggregation.ACS central science · 2025Article
- Article
- In the flow, how fluid dynamics shapes amyloid formation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Aggregation of α-synuclein splice isoforms through a phase separation pathway.Science advances · 2025Article
- Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024Review
- Aggregation of the amyloid-β peptide (Aβ40) within condensates generated through liquid-liquid phase separation.Scientific reports · 2024Article
- Formation of Nanofibrillar Self-Healing Hydrogels Using Antimicrobial Peptides.ACS applied materials & interfaces · 2024Article
- Preparation and Characterization of Zn(II)-Stabilized AβACS chemical neuroscience · 2024Article
- High-throughput and proteome-wide discovery of endogenous biomolecular condensates.Nature chemistry · 2024Article
- Modulation of α-synuclein in vitro aggregation kinetics by its alternative splice isoforms.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The liquid-to-solid transition of FUS is promoted by the condensate surface.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
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Authors and funding
9 authors.
Funding
Abstract
Primary nucleation is the fundamental event that initiates the conversion of proteins from their normal physiological forms into pathological amyloid aggregates associated with the onset and development of disorders including systemic amyloidosis, as well as the neurodegenerative conditions Alzheimer's and Parkinson's diseases. It has become apparent that the presence of surfaces can dramatically modulate nucleation. However, the underlying physicochemical parameters governing this process have been challenging to elucidate, with interfaces in some cases having been found to accelerate aggregation, while in others they can inhibit the kinetics of this process. Here we show through kinetic analysis that for three different fibril-forming proteins, interfaces affect the aggregation reaction mainly through modulating the primary nucleation step. Moreover, we show through direct measurements of the Gibbs free energy of adsorption, combined with theory and coarse-grained computer simulations, that overall nucleation rates are suppressed at high and at low surface interaction strengths but significantly enhanced at intermediate strengths, and we verify these regimes experimentally. Taken together, these results provide a quantitative description of the fundamental process which triggers amyloid formation and shed light on the key factors that control this process.
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