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- W3136010136 abstract "Defective protein folding and accumulation of misfolded proteins is associated with neurodegenerative, cardiovascular, secretory, and metabolic disorders. Efforts are being made to identify small-molecule modulators or structural-correctors for conformationally destabilized proteins implicated in various protein aggregation diseases. Using a metastable-reporter-based primary screen, we evaluated pharmacological chaperone activity of a diverse class of natural products. We found that a flavonoid glycoside (C-10, chrysoeriol-7-O-β-D-glucopyranoside) stabilizes metastable proteins, prevents its aggregation, and remodels the oligomers into protease-sensitive species. Data was corroborated with additional secondary screen with disease-specific pathogenic protein. In vitro and cell-based experiments showed that C-10 inhibits α-synuclein aggregation which is implicated in synucleinopathies-related neurodegeneration. C-10 interferes in its structural transition into β-sheeted fibrils and mitigates α-synuclein aggregation-associated cytotoxic effects. Computational modeling suggests that C-10 binds to unique sites in α-synuclein which may interfere in its aggregation amplification. These findings open an avenue for comprehensive SAR development for flavonoid glycosides as pharmacological chaperones for metastable and aggregation-prone proteins implicated in protein conformational diseases." @default.
- W3136010136 created "2021-03-29" @default.
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- W3136010136 date "2021-05-04" @default.
- W3136010136 modified "2023-10-16" @default.
- W3136010136 title "Identification of Natural Products as Potential Pharmacological Chaperones for Protein Misfolding Diseases." @default.
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- W3136010136 doi "https://doi.org/10.1002/cmdc.202100147" @default.
- W3136010136 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33760394" @default.
- W3136010136 hasPublicationYear "2021" @default.
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