ArticleProtein science : a publication of the Protein Society2019
Suppression, disaggregation, and modulation of γ-Synuclein fibrillation pathway by green tea polyphenol EGCG.
Article in Protein science : a publication of the Protein Society, 2019. 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.
- An integrative analysis combining bioinformatics, network pharmacology and experimental methods identified key genes of EGCG targets in Nasopharyngeal Carcinoma.Discover oncology · 2025Article
- Inhibition of amyloid formation of prion fragment (106-128) by polyphenolic compounds.Biochimica et biophysica acta. General subjects · 2025Article
- Investigating lysozyme amyloid fibril formation and structural variability dependence on its initial folding state under different pH conditions.Protein science : a publication of the Protein Society · 2024Article
- Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates.Nature communications · 2023Article
- Review
- Amyloid Disassembly: What Can We Learn from Chaperones?Biomedicines · 2022Review
- Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties.Antioxidants (Basel, Switzerland) · 2022Article
- Epigallocatechin-3-gallate: A phytochemical as a promising drug candidate for the treatment of Parkinson's disease.Frontiers in pharmacology · 2022Review
- Genome-Wide Methylation Profiling in the Thalamus of Scrapie Sheep.Frontiers in veterinary science · 2022Article
- Anti-Biofilm Molecules Targeting Functional Amyloids.Antibiotics (Basel, Switzerland) · 2021Review
- Pentameric Thiophene as a Probe to Monitor EGCG's Remodeling Activity of Mature Amyloid Fibrils: Overcoming Signal Artifacts of Thioflavin T.ACS omega · 2021Article
- Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity.International journal of molecular sciences · 2020Article
- Antibiofilm activity of flavonoids on staphylococcal biofilms through targeting BAP amyloids.Scientific reports · 2020Article
- Dietary Antioxidants and Parkinson's Disease.Antioxidants (Basel, Switzerland) · 2020Review
- The Aggregation Conditions Define Whether EGCG is an Inhibitor or Enhancer ofInternational journal of molecular sciences · 2020Article
- The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG.Biomolecules · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Oligomerization of γ-Synuclein is known to have implications for both neurodegeneration and cancer. Although it is known to co-exist with the fibrillar deposits of α-Synuclein (Lewy bodies), a hallmark in Parkinson's disease (PD), the effect of potential therapeutic modulators on the fibrillation pathway of γ-Syn remains unexplored. By a combined use of various biophysical tools and cytotoxicity assays we demonstrate that the flavonoid epigallocatechin-3-gallate (EGCG) significantly suppresses γ-Syn fibrillation by affecting its nucleation and binds with the unstructured, nucleus forming oligomers of γ-Syn to modulate the pathway to form α-helical containing higher-order oligomers (~158 kDa and ~ 670 kDa) that are SDS-resistant and conformationally restrained in nature. Seeding studies reveal that these oligomers although "on-pathway" in nature, are kinetically retarded and rate-limiting species that slows down fibril elongation. We observe that EGCG also disaggregates the protofibrils and mature γ-Syn fibrils into similar SDS-resistant oligomers. Steady-state and time-resolved fluorescence spectroscopy and isothermal titration calorimetry (ITC) reveal a weak non-covalent interaction between EGCG and γ-Syn with the dissociation constant in the mM range (K
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Registered trials
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