ArticleProceedings of the National Academy of Sciences of the United States of America2021
The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Microfluidics for protein interaction studies: current methods, challenges, and future perspectives.European biophysics journal : EBJ · 2026Review
- Small heat shock protein HSPB8 interacts with a pre-fibrillar TDP43 low complexity domain species to delay fibril formation.Biophysical chemistry · 2026Article
- Chaperone proteins protect against desmin fragment amyloid aggregation.Biophysical journal · 2026Article
- Using a stable protein scaffold to display peptides that bind to alpha-synuclein fibrils.Protein science : a publication of the Protein Society · 2025Article
- Single-molecule observations of human small heat shock proteins in complex with aggregation-prone client proteins.The Biochemical journal · 2025Article
- The Detection of Toxic Amyloid-β Fibril Fragments Through a Surface Plasmon Resonance Immunoassay.International journal of molecular sciences · 2024Article
- Modulation of Alzheimer's Disease Aβ40 Fibril Polymorphism by the Small Heat Shock Protein αB-Crystallin.Journal of the American Chemical Society · 2024Article
- Dissecting the Self-assembly Dynamics of Imperfect Repeats in α-Synuclein.Journal of chemical information and modeling · 2023Article
- Short hydrophobic loop motifs in BRICHOS domains determine chaperone activity against amorphous protein aggregation but not against amyloid formation.Communications biology · 2023Article
- Non-specificity as the sticky problem in therapeutic antibody development.Nature reviews. Chemistry · 2022Review
- General Theory of Specific Binding: Insights from a Genetic-Mechano-Chemical Protein Model.Molecular biology and evolution · 2022Article
- Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen PhosphorylaseInternational journal of molecular sciences · 2022Article
- The role of heat shock proteins in preventing amyloid toxicity.Frontiers in molecular biosciences · 2022Review
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Authors and funding
16 authors at 2 institutions in 2 countries.
Funding
Abstract
Molecular chaperones are key components of the cellular proteostasis network whose role includes the suppression of the formation and proliferation of pathogenic aggregates associated with neurodegenerative diseases. The molecular principles that allow chaperones to recognize misfolded and aggregated proteins remain, however, incompletely understood. To address this challenge, here we probe the thermodynamics and kinetics of the interactions between chaperones and protein aggregates under native solution conditions using a microfluidic platform. We focus on the binding between amyloid fibrils of α-synuclein, associated with Parkinson's disease, to the small heat-shock protein αB-crystallin, a chaperone widely involved in the cellular stress response. We find that αB-crystallin binds to α-synuclein fibrils with high nanomolar affinity and that the binding is driven by entropy rather than enthalpy. Measurements of the change in heat capacity indicate significant entropic gain originates from the disassembly of the oligomeric chaperones that function as an entropic buffer system. These results shed light on the functional roles of chaperone oligomerization and show that chaperones are stored as inactive complexes which are capable of releasing active subunits to target aberrant misfolded species.
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