ArticleBMC complementary medicine and therapies2020
Inhibition of alpha-synuclein seeded fibril formation and toxicity by herbal medicinal extracts.
Article in BMC complementary medicine and therapies, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 17 papers.
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17 citing papers in PubMed, 33 citations in OpenAlex.
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- Pharmacological mechanisms and potential clinical applications of Dihydromyricetin in neurological disorders.Frontiers in pharmacology · 2025Review
- SIRT3 enhances the protective effect of Xyloketal B on seizure-induced brain injury by regulating AMPK/mTOR signaling-mediated autophagy.The Kaohsiung journal of medical sciences · 2024Article
- Cell membrane proteome analysis in HEK293T cells challenged with α-synuclein amyloids.Journal of biosciences · 2024Article
- The potential of natural products to inhibit abnormal aggregation of α-Synuclein in the treatment of Parkinson's disease.Frontiers in pharmacology · 2024Review
- Pyrogallol, Corilagin and Chebulagic acid target the "fuzzy coat" of alpha-synuclein to inhibit the fibrillization of the protein.RSC advances · 2022Article
- Insights into the Explicit Protective Activity of Herbals in Management of Neurodegenerative and Cerebrovascular Disorders.Molecules (Basel, Switzerland) · 2022Review
- α-Synuclein phosphorylation at serine 129 occurs after initial protein deposition and inhibits seeded fibril formation and toxicity.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The role of the endolysosomal pathway in α-synuclein pathogenesis in Parkinson's disease.Frontiers in cellular neuroscience · 2022Review
- Nanotechnology-Based Drug Delivery Strategies to Repair the Mitochondrial Function in Neuroinflammatory and Neurodegenerative Diseases.Pharmaceutics · 2021Review
- Acetylcholinesterase Inhibitors in the Treatment of Neurodegenerative Diseases and the Role of Acetylcholinesterase in their Pathogenesis.International journal of molecular sciences · 2021Review
- Study effect of Baicalein encapsulated/loaded Chitosan-nanoparticle on allergic Asthma pathology in mouse model.Saudi journal of biological sciences · 2021Article
- Natural Alkaloid Compounds as Inhibitors for Alpha-Synuclein Seeded Fibril Formation and Toxicity.Molecules (Basel, Switzerland) · 2021Article
- A Triple Role for a Bilayer: Using Nanoliposomes to Cross and Protect Cellular Membranes.The Journal of membrane biology · 2021Article
- Baicalein Ameliorates Aβ-Induced Memory Deficits and Neuronal AtrophyFrontiers in pharmacology · 2021Article
- Article
Corrections and comments
- Retracted
Authors and funding
12 authors at 8 institutions in 6 countries.
Funding
Abstract
backgroundRecent studies indicated that seeded fibril formation and toxicity of α-synuclein (α-syn) play a main role in the pathogenesis of certain diseases including Parkinson's disease (PD), multiple system atrophy, and dementia with Lewy bodies. Therefore, examination of compounds that abolish the process of seeding is considered a key step towards therapy of several synucleinopathies.
methodsUsing biophysical, biochemical and cell-culture-based assays, assessment of eleven compounds, extracted from Chinese medicinal herbs, was performed in this study for their effect on α-syn fibril formation and toxicity caused by the seeding process.
resultsSalvianolic acid B and dihydromyricetin were the two compounds that strongly inhibited the fibril growth and neurotoxicity of α-syn. In an in-vitro cell model, these compounds decreased the insoluble phosphorylated α-syn and aggregation. Also, in primary neuronal cells, these compounds showed a reduction in α-syn aggregates. Both compounds inhibited the seeded fibril growth with dihydromyricetin having the ability to disaggregate preformed α-syn fibrils. In order to investigate the inhibitory mechanisms of these two compounds towards fibril formation, we demonstrated that salvianolic acid B binds predominantly to monomers, while dihydromyricetin binds to oligomeric species and to a lower extent to monomers. Remarkably, these two compounds stabilized the soluble non-toxic oligomers lacking β-sheet content after subjecting them to proteinase K digestion.
conclusionsEleven compounds were tested but only two showed inhibition of α-syn aggregation, seeded fibril formation and toxicity in vitro. These findings highlight an essential beginning for development of new molecules in the field of synucleinopathies treatment.
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