ArticleOxidative medicine and cellular longevity2018
Inhibition of Protein Aggregation by Several Antioxidants.
Article in Oxidative medicine and cellular longevity, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Complexation of Hen Egg White Lysozyme With Bioactive Phenolic Acids: Molecular Insights Into the Binding Mechanisms and Inhibitory Effects Against Protein Aggregation.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Eugenol from Syzygium aromaticum enhances longevity and proteostasis in aged yeast.Biogerontology · 2026Article
- Review
- 1-Mesityl-3-(3-Sulfonatopropyl) Imidazolium Protects Against Oxidative Stress and Delays Proteotoxicity inFrontiers in pharmacology · 2022Article
- Human stefin B: from its structure, folding, and aggregation to its function in health and disease.Frontiers in molecular neuroscience · 2022Review
- Dual concentration-dependent effect of ascorbic acid on PAP(248-286) amyloid formation and SEVI-mediated HIV infection.RSC chemical biology · 2021Article
- Synergy of the Inhibitory Action of Polyphenols Plus Vitamin C on Amyloid Fibril Formation: Case Study of Human Stefin B.Antioxidants (Basel, Switzerland) · 2021Article
- Review
- Modulating disease-relevant tau oligomeric strains by small molecules.The Journal of biological chemistry · 2020Article
- Review
- Toxic Tau Oligomers Modulated by Novel Curcumin Derivatives.Scientific reports · 2019Article
- WS-5 Extract ofEvidence-based complementary and alternative medicine : eCAM · 2019Article
- Development and In Vitro Evaluation of Linear PEI-Shelled Heparin/Berberine Nanoparticles in Human Osteosarcoma U-2 OS Cells.Molecules (Basel, Switzerland) · 2018Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibril formation is a shared property of all proteins; therefore, model proteins can be used to study this process. We measured protein aggregation of the model amyloid-forming protein stefin B in the presence and absence of several antioxidants. Amyloid fibril formation by stefin B was routinely induced at pH 5 and 10% TFE, at room temperature. The effects of antioxidants NAC, vitamin C, vitamin E, and the three polyphenols resveratrol, quercetin, and curcumin on the kinetics of fibril formation were followed using ThT fluorescence. Concomitantly, the morphology and amount of the aggregates and fibrils were checked by transmission electron microscopy (TEM). The concentration of the antioxidants was varied, and it was observed that different modes of action apply at low or high concentrations relative to the binding constant. In order to obtain more insight into the possible mode of binding, docking of NAC, vitamin C, and all three polyphenols was done to the monomeric form of stefin B.
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