ArticleScientific reports2016
Effect of curcumin analogs onα-synuclein aggregation and cytotoxicity.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 65 citations in OpenAlex.
- Modulation of α-Synuclein Fibrillation and Toxicity by 4-Phenylbutyric Acid.ACS chemical neuroscience · 2025Article
- Gut-Brain Axis in Focus: Polyphenols, Microbiota, and Their Influence on α-Synuclein in Parkinson's Disease.Nutrients · 2024Review
- Curcumin Inhibits α-Synuclein Aggregation by Acting on Liquid-Liquid Phase Transition.Foods (Basel, Switzerland) · 2024Article
- The potential of natural products to inhibit abnormal aggregation of α-Synuclein in the treatment of Parkinson's disease.Frontiers in pharmacology · 2024Review
- High Yield Synthesis of Curcumin and Symmetric Curcuminoids: A "Click" and "Unclick" Chemistry Approach.Molecules (Basel, Switzerland) · 2022Article
- Phytochemical Composition, Antimicrobial, Anticancer Properties, and Antioxidant Potential of Green Husk from Several Walnut Varieties (Antioxidants (Basel, Switzerland) · 2022Article
- Pyrogallol, Corilagin and Chebulagic acid target the "fuzzy coat" of alpha-synuclein to inhibit the fibrillization of the protein.RSC advances · 2022Article
- Catechol-containing compounds are a broad class of protein aggregation inhibitors: Redox state is a key determinant of the inhibitory activities.Pharmacological research · 2022Article
- Curcumin Interacts with α-Synuclein Condensates To Inhibit Amyloid Aggregation under Phase Separation.ACS omega · 2022Article
- Disease-modifying treatment of Parkinson's disease by phytochemicals: targeting multiple pathogenic factors.Journal of neural transmission (Vienna, Austria : 1996) · 2022Review
- Haplotype-resolved genome of diploid ginger (Zingiber officinale) and its unique gingerol biosynthetic pathway.Horticulture research · 2021Article
- Broadening the scope of high structural dimensionality nanomaterials using pyridine-based curcuminoids.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Dietary Polyphenols in Metabolic and Neurodegenerative Diseases: Molecular Targets in Autophagy and Biological Effects.Antioxidants (Basel, Switzerland) · 2021Review
- Ophthalmic Biomarkers for Alzheimer's Disease: A Review.Frontiers in aging neuroscience · 2021Review
- Natural and Synthetic Derivatives of Hydroxycinnamic Acid Modulating the Pathological Transformation of Amyloidogenic Proteins.Molecules (Basel, Switzerland) · 2020Review
- Dietary Antioxidants and Parkinson's Disease.Antioxidants (Basel, Switzerland) · 2020Review
- Advances in protein misfolding, amyloidosis and its correlation with human diseases.3 Biotech · 2020Review
- Soluble endogenous oligomeric α-synuclein species in neurodegenerative diseases: Expression, spreading, and cross-talk.Journal of Parkinson's disease · 2020Review
- Triphala inhibits alpha-synuclein fibrillization and their interaction study by NMR provides insights into the self-association of the protein.RSC advances · 2019Article
- Cell-Based Screen Using Amyloid Mimic β23 Expression Identifies Peucedanocoumarin III as a Novel Inhibitor of α-Synuclein and Huntingtin Aggregates.Molecules and cells · 2019Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alpha-synuclein (α-Syn) aggregation into oligomers and fibrils is associated with dopaminergic neuron loss occurring in Parkinson's disease (PD) pathogenesis. Compounds that modulate α-Syn aggregation and interact with preformed fibrils/oligomers and convert them to less toxic species could have promising applications in the drug development efforts against PD. Curcumin is one of the Asian food ingredient which showed promising role as therapeutic agent against many neurological disorders including PD. However, the instability and low solubility makes it less attractive for the drug development. In this work, we selected various curcumin analogs and studied their toxicity, stability and efficacy to interact with different α-Syn species and modulation of their toxicity. We found a subset of curcumin analogs with higher stability and showed that curcumin and its various analogs interact with preformed fibrils and oligomers and accelerate α-Syn aggregation to produce morphologically different amyloid fibrils in vitro. Furthermore, these curcumin analogs showed differential binding with the preformed α-Syn aggregates. The present data suggest the potential role of curcumin analogs in modulating α-Syn aggregation.
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