ArticleCurrent research in structural biology2020
Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism.
Article in Current research in structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Thermodynamic Frontiers in Hemoglobin-Inspired Polymer Science for Diagnosis and Modulation of Neurodegenerative Diseases.Cell biochemistry and function · 2026Review
- Cosolutes Modulate Polyubiquitin Fibrillation.ACS omega · 2026Article
- Charge-Based Discrimination of Amyloids Using an Amyloid-Targeting Chemiluminescent Probe.Chembiochem : a European journal of chemical biology · 2026Article
- Metal-Resistant Mesophilic Laccase from Achromobacter Species: Identification, Physical Characterisation, and Dye Bioremediation.Applied biochemistry and biotechnology · 2026Article
- Investigating Local Sequence-Structural Attributes of Amyloidogenic Light Chain Variable Domains.Proteins · 2025Article
- Conformational Switch in the Alpha-Synuclein C-Terminal Domain Directs Its Fibril Polymorphs.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Accelerated amyloid fibril formation at the interface of liquid-liquid phase-separated droplets by depletion interactions.Protein science : a publication of the Protein Society · 2025Article
- Discovery of potent inhibitors of α-synuclein aggregation using structure-based iterative learning.Nature chemical biology · 2024Article
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Light, Water, and Melatonin: The Synergistic Regulation of Phase Separation in Dementia.International journal of molecular sciences · 2023Review
- Mechanisms of polyphosphate-induced amyloid fibril formation triggered by breakdown of supersaturation.Biophysics and physicobiology · 2023Article
- pH Dependence of Amyloid-β Fibril Assembly Kinetics: Unravelling the Microscopic Molecular Processes.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- pH Dependence of Amyloid-β Fibril Assembly Kinetics: Unravelling the Microscopic Molecular Processes.Angewandte Chemie (International ed. in English) · 2022Article
- Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022Review
- Polyphenol-solubility alters amyloid fibril formation of α-synuclein.Protein science : a publication of the Protein Society · 2021Article
- Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners.The Journal of biological chemistryArticle
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins in either a native or denatured conformation often aggregate at an isoelectric point (pI), a phenomenon known as pI precipitation. However, only a few studies have addressed the role of pI precipitation in amyloid formation, the crystal-like aggregation of denatured proteins. We found that α-synuclein, an intrinsically disordered protein of 140 amino acid residues associated with Parkinson's disease, formed amyloid fibrils at pI (= 4.7) under the low-sodium phosphate conditions. Although α-synuclein also formed amyloid fibrils at a wide pH range under high concentrations of sodium phosphate, the pI-amyloid formation was characterized by marked amyloid-specific thioflavin T fluorescence and clear fibrillar morphology, indicating highly ordered structures. Analysis by heteronuclear NMR in combination with principal component analysis suggested that amyloid formation under low and high phosphate conditions occurred by distinct mechanisms. The former was likely to be caused by the intermolecular attractive charge-charge interactions, where α-synuclein has +17 and -17 charges even with the zero net charge. On the other hand, the latter was caused by the phosphate-dependent salting-out effects. pI-amyloid formation may play a role in the membrane-dependent amyloid formation of α-synuclein, where the negatively charged membrane surface reduces the local pH to pI and the membrane hydrophobic environment enhances electrostatic interactions. The results extend the supersaturation-limited mechanism of amyloid formation: Amyloid fibrils are formed under a variety of conditions of decreased solubility of denatured proteins triggered by the breakdown of supersaturation.
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