ArticleScientific reports2020
Gallic acid oxidation products alter the formation pathway of insulin amyloid fibrils.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 26 citations in OpenAlex.
- Bioinformatics Tools for the Analysis of Active Compounds Identified in Ranunculaceae Species.Pharmaceuticals (Basel, Switzerland) · 2023Article
- The Major Components of Cerebrospinal Fluid Dictate the Characteristics of Inhibitors against Amyloid-Beta Aggregation.International journal of molecular sciences · 2023Article
- Characterization of Orange Peel Extract and Its Potential Protective Effect against Aluminum Chloride-Induced Alzheimer's Disease.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Roles of traditional chinese medicine regulating neuroendocrinology on AD treatment.Frontiers in endocrinology · 2022Review
- Autoxidation Enhances Anti-Amyloid Potential of Flavone Derivatives.Antioxidants (Basel, Switzerland) · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
Amyloidogenic protein assembly into insoluble fibrillar aggregates is linked with several neurodegenerative disorders, such as Alzheimer's or Parkinson's disease, affecting millions of people worldwide. The search for a potential anti-amyloid drug has led to the discovery of hundreds of compounds, none of which have passed all clinical trials. Gallic acid has been shown to both modulate factors leading to the onset of neurodegenerative disorders, as well as directly inhibit amyloid formation. However, the conditions under which this effect is seen could lead to oxidation of this polyphenol, likely changing its properties. Here we examine the effect of gallic acid and its oxidised form on the aggregation of a model amyloidogenic protein-insulin at low pH conditions. We show a vastly higher inhibitory potential of the oxidised form, as well as an alteration in the aggregation pathway, leading to the formation of a specific fibril conformation.
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