ArticleInternational journal of molecular sciences2020
The Aggregation Conditions Define Whether EGCG is an Inhibitor or Enhancer of
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 37 citations in OpenAlex.
- Article
- The amplification of α-synuclein amyloid fibrils.Biochemical Society transactions · 2026Review
- Inhibitory effect of epigallocatechin-3-gallate as a potent anti-amyloidogenic agent against the G138E mutant of SOD1.Scientific reports · 2026Article
- Neuroactive Phytochemicals as Multi-Target Modulators of Mental Health and Cognitive Function: An Integrative Review.International journal of molecular sciences · 2025Review
- Navigation Between Alzheimer's Disease (AD) and Its Various Pathophysiological Trajectories: The Pathogenic Link to Neuroimmunology-Genetics and Neuroinflammation.International journal of molecular sciences · 2025Review
- Epigallocatechin-3-gallate binds tandem RNA recognition motifs of TDP-43 and inhibits its aggregation.Scientific reports · 2025Article
- Molecular mechanisms underlying the neuroprotective effects of polyphenols: implications for cognitive function.EXCLI journal · 2025Review
- Study of Insulin Aggregation and Fibril Structure under Different Environmental Conditions.International journal of molecular sciences · 2024Article
- The potential of natural products to inhibit abnormal aggregation of α-Synuclein in the treatment of Parkinson's disease.Frontiers in pharmacology · 2024Review
- Bioactive Compounds and Their Influence on Postnatal Neurogenesis.International journal of molecular sciences · 2023Review
- Natural Inhibitors of Amyloid Aggregation.International journal of molecular sciences · 2023Article
- The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation.International journal of molecular sciences · 2023Review
- Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models.International journal of molecular sciences · 2022Review
- Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties.Antioxidants (Basel, Switzerland) · 2022Article
- Stability matters, too - the thermodynamics of amyloid fibril formation.Chemical science · 2022Review
- Epigallocatechin-3-Gallate (EGCG): New Therapeutic Perspectives for Neuroprotection, Aging, and Neuroinflammation for the Modern Age.Biomolecules · 2022Review
- Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration.International journal of molecular sciences · 2021Article
- Green Tea Epigallocatechin-3-gallate (EGCG) Targeting Protein Misfolding in Drug Discovery for Neurodegenerative Diseases.Biomolecules · 2021Review
- A Triple Role for a Bilayer: Using Nanoliposomes to Cross and Protect Cellular Membranes.The Journal of membrane biology · 2021Article
- Green Tea Polyphenol Epigallocatechin-Gallate in Amyloid Aggregation and Neurodegenerative Diseases.Frontiers in neuroscience · 2021Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
The amyloid fibril formation by α -synuclein is a hallmark of various neurodegenerative disorders, most notably Parkinson's disease. Epigallocatechin gallate (EGCG) has been reported to be an efficient inhibitor of amyloid formation by numerous proteins, among them α -synuclein. Here, we show that this applies only to a small region of the relevant parameter space, in particular to solution conditions where EGCG readily oxidizes, and we find that the oxidation product is a much more potent inhibitor compared to the unmodified EGCG. In addition to its inhibitory effects, EGCG and its oxidation products can under some conditions even accelerate α -synuclein amyloid fibril formation through facilitating its heterogeneous primary nucleation. Furthermore, we show through quantitative seeding experiments that, contrary to previous reports, EGCG is not able to re-model α -synuclein amyloid fibrils into seeding-incompetent structures. Taken together, our results paint a complex picture of EGCG as a compound that can under some conditions inhibit the amyloid fibril formation of α -synuclein, but the inhibitory action is not robust against various physiologically relevant changes in experimental conditions. Our results are important for the development of strategies to identify and characterize promising amyloid inhibitors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.