ArticleScientific reports2016
Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 47 citations in OpenAlex.
- Formation of Condition-Dependent Alpha-Synuclein Fibril Strain in Artificial Cerebrospinal Fluid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Early diagnosis of Parkinson's disease using split aptamer-based lateral flow assay with saliva sample.Mikrochimica acta · 2025Article
- Pathological Disulfide Bond Crosslinking: Molecular Insights into Amyloidogenesis and Diseases Progression.Chembiochem : a European journal of chemical biology · 2025Review
- Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation.Journal of advanced research · 2025Review
- Probing the structural stability of R-phycocyanin under pressure.Protein science : a publication of the Protein Society · 2024Article
- The effects of biological crowders on fibrillization, structure, diffusion, and conformational dynamics of α-synuclein.Protein science : a publication of the Protein Society · 2024Article
- Familial Alzheimer's Disease-Related Mutations Differentially Alter Stability of Amyloid-Beta Aggregates.The journal of physical chemistry letters · 2023Article
- Stability matters, too - the thermodynamics of amyloid fibril formation.Chemical science · 2022Review
- Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy.RSC chemical biology · 2021Article
- Comprehensive Structural and Thermodynamic Analysis of Prefibrillar WT α-Synuclein and Its G51D, E46K, and A53T Mutants by a Combination of Small-Angle X-ray Scattering and Variational Bayesian Weighting.Journal of chemical information and modeling · 2020Article
- Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism.Current research in structural biology · 2020Article
- High-Pressure Response of Amyloid Folds.Viruses · 2019Review
- Alpha-synuclein stepwise aggregation reveals features of an early onset mutation in Parkinson's disease.Communications biology · 2019Article
- Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein.Journal of molecular biology · 2018Article
- A Protofilament-Protofilament Interface in the Structure of Mouse α-Synuclein Fibrils.Biophysical journal · 2018Article
- High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy.Biophysical journal · 2017Article
- Water Distribution, Dynamics, and Interactions with Alzheimer's β-Amyloid Fibrils Investigated by Solid-State NMR.Journal of the American Chemical Society · 2017Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Parkinson's disease is a neurological disease in which aggregated forms of the α-synuclein (α-syn) protein are found. We used high hydrostatic pressure (HHP) coupled with NMR spectroscopy to study the dissociation of α-syn fibril into monomers and evaluate their structural and dynamic properties. Different dynamic properties in the non-amyloid-β component (NAC), which constitutes the Greek-key hydrophobic core, and in the acidic C-terminal region of the protein were identified by HHP NMR spectroscopy. In addition, solid-state NMR revealed subtle differences in the HHP-disturbed fibril core, providing clues to how these species contribute to seeding α-syn aggregation. These findings show how pressure can populate so far undetected α-syn species, and they lay out a roadmap for fibril dissociation via pathways not previously observed using other approaches. Pressure perturbs the cavity-prone hydrophobic core of the fibrils by pushing water inward, thereby inducing the dissociation into monomers. Our study offers the molecular details of how hydrophobic interaction and the formation of water-excluded cavities jointly contribute to the assembly and stabilization of the fibrils. Understanding the molecular forces behind the formation of pathogenic fibrils uncovered by pressure perturbation will aid in the development of new therapeutics against Parkinson's disease.
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