ArticlePloS one2017
Inhibition of HEWL fibril formation by taxifolin: Mechanism of action.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.
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Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.
- Insights into the Pharmacological Effects of Flavonoids: The Systematic Review of Computer Modeling.International journal of molecular sciences · 2022Pooled it
- Peroxynitrite-induced structural remodeling and aggregation of hemoglobin under nitroxidative stress.Protein science : a publication of the Protein Society · 2026Article
- Protein Recognition and Amyloid Remodeling Governed by Paddlewheel Diruthenium Coordination Chemistry.Inorganic chemistry · 2026Article
- Inhibition of cytotoxic fibril formation of α-synuclein and human insulin by Silymarin from the Silybum marianum.PloS one · 2025Article
- Inhibition of cytotoxic self-assembly of HEWL through promoting fibrillation by new synthesized α-hydroxycarbamoylphosphinic acids.RSC advances · 2024Article
- The inhibition of fibril formation of lysozyme by sucrose and trehalose.RSC advances · 2024Article
- The Ability of Some Polysaccharides to Disaggregate Lysozyme Amyloid Fibrils and Renature the Protein.Pharmaceutics · 2023Article
- New Perspectives of Taxifolin in Neurodegenerative Diseases.Current neuropharmacology · 2023Review
- Bivalent metal ions induce formation of α-synuclein fibril polymorphs with different cytotoxicities.Scientific reports · 2022Article
- Natural product-based radiopharmaceuticals: Focus on curcumin and its analogs, flavonoids, and marine peptides.Journal of pharmaceutical analysis · 2022Review
- Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg-white lysozyme.Veterinary medicine and science · 2021Article
- Bioactive Phytocompounds: Anti-amyloidogenic Effects Against Hen Egg-White Lysozyme Aggregation.The protein journal · 2021Article
- The In Vitro Anti-amyloidogenic Activity of the Mediterranean Red SeaweedPharmaceuticals (Basel, Switzerland) · 2020Article
- Advances in protein misfolding, amyloidosis and its correlation with human diseases.3 Biotech · 2020Review
- Role of surface oxygen-containing functional groups of graphene oxide quantum dots on amyloid fibrillation of two model proteins.PloS one · 2020Article
- α-synuclein interaction with zero-valent iron nanoparticles accelerates structural rearrangement into amyloid-susceptible structure with increased cytotoxic tendency.International journal of nanomedicine · 2019Article
- Vitamin K1 As A Potential Molecule For Reducing Single-Walled Carbon Nanotubes-Stimulated α-Synuclein Structural Changes And Cytotoxicity.International journal of nanomedicine · 2019Article
- Cerium oxide NPs mitigate the amyloid formation of α-synuclein and associated cytotoxicity.International journal of nanomedicine · 2019Article
- Amorphous aggregation of tau in the presence of titanium dioxide nanoparticles: biophysical, computational, and cellular studies.International journal of nanomedicine · 2019Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among therapeutic approaches for amyloid-related diseases, attention has recently turned to the use of natural products as effective anti-aggregation compounds. Although a wealth of in vitro and in vivo evidence indicates some common inhibitory activity of these compounds, they don't generally suggest the same mechanism of action. Here, we show that taxifolin, a ubiquitous bioactive constituent of foods and herbs, inhibits formation of HEWL amyloid fibrils and their related toxicity by causing formation of very large globular, chain-like aggregates. A range of amyloid-specific techniques were employed to characterize this process. We found that taxifolin exerts its effect by binding to HEWL prefibrillar species, rather than by stabilizing the molecule in its native-like state. Furthermore, it's binding results in diverting the amyloid pathway toward formation of very large globular, chain-like aggregates with low β-sheet content and reduced solvent-exposed hydrophobic patches. ThT fluorescence measurements show that the binding capacity of taxifolin is significantly reduced, upon generation of large protofibrillar aggregates at the end of growth phase. We believe these results may help design promising inhibitors of protein aggregation for amyloid-related diseases.
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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.