ArticlePloS one2019
The interaction of several herbal extracts with α-synuclein: Fibril formation and surface plasmon resonance analysis.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 27 citations in OpenAlex.
- Inhibition of cytotoxic fibrillation of human insulin using silver nanoparticles capped by aqueous extract of Echium amoenum.Scientific reports · 2025Article
- Therapeutic Potential of Pistachio Green Hull Extract in Treating Parkinson's Disease: A Comprehensive In Vivo and In Vitro Investigation.Food science & nutrition · 2025Article
- Exploring the Potential of Biomimetic Peptides in Targeting Fibrillar and Filamentous Alpha-Synuclein-An In Silico and Experimental Approach to Parkinson's Disease.Biomimetics (Basel, Switzerland) · 2024Article
- Efficient characterization of multiple binding sites of small molecule imaging ligands on amyloid-beta, tau and alpha-synuclein.European journal of nuclear medicine and molecular imaging · 2024Article
- Comprehensive Evaluation of the Bioactive Composition and Neuroprotective and Antimicrobial Properties of Vacuum-Dried Broccoli (Molecules (Basel, Switzerland) · 2023Article
- Single point mutations at the S129 residue of α-synuclein and their effect on structure, aggregation, and neurotoxicity.Frontiers in chemistry · 2023Article
- Pyrogallol, Corilagin and Chebulagic acid target the "fuzzy coat" of alpha-synuclein to inhibit the fibrillization of the protein.RSC advances · 2022Article
- Peppermint extract inhibits protein aggregation.Biologia futura · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins from their native conformation convert into highly ordered fibrillar aggregation under particular conditions; that are described as amyloid fibrils. α-Synuclein (α-Syn) is a small natively unfolded protein that its fibrillation is the causative factor of Parkinson's disease. One important approach in the development of therapeutic agents is the use of small molecules (such as flavonoids) that could specifically and efficiently inhibit the aggregation process. In this study the effect of few herbal extract (Berberis, Quercus robur, Zizyphus vulgaris, Salix aegyptica) containing flavonoids were investigated on fibril formation of α-syn by using conventional methods such as ThT fluorescence, circular dichroism (CD) spectroscopy and transmission electron microscopy (TEM). The interaction of extracts were also analysed by surface plasmon resonance (SPR). Among extracts, Salix aegyptica revealed the highest inhibitory effect on fibril formation. As expected, Salix aegyptica extract also exhibited the highest affinity toward α-syn. Cell viability using MTT assay revealed that fibrils alone were more toxic than those containing the extract. Overall, we demonstrated that the affinity of compounds used in this study corresponds to their ability to arrest fibrillation and reduce cellular toxicity of α-syn fibrils.
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