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- W2472839807 abstract "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." @default.
- W2472839807 created "2016-07-22" @default.
- W2472839807 creator A5013425190 @default.
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- W2472839807 date "2016-06-24" @default.
- W2472839807 modified "2023-10-16" @default.
- W2472839807 title "Effect of curcumin analogs onα-synuclein aggregation and cytotoxicity" @default.
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- W2472839807 doi "https://doi.org/10.1038/srep28511" @default.
- W2472839807 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4919791" @default.
- W2472839807 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27338805" @default.
- W2472839807 hasPublicationYear "2016" @default.
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