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- W2479581917 abstract "Background: The amassing of β- sheet rich amyloid fibrils is complex, multistep process which is allied with cellular toxicity in number of human protein misfolding diseases including Parkinson's, Alzheimer's and systemic amyloidosis. Methodology: In vitro aggregation of lysozyme was induced by incubation for 3 days at 60 degrees C and monitored by ThT binding assay, Congo red binding, ANS binding circular dichroism and electron microscopy. Results: Menadione inhibits the fibrillogenesis of lysozyme by directly binding to lysozyme and preventing their conversion to toxic aggregates and modulates amyloid cytotoxicity against human neuroblastoma cell line (SH-SY5Y) which confirmed the anti-amyloidogenic behaviour of menadione. Importantly, it was found that menadione remodel preformed amyloids to less toxic amorphous aggregates with less cross beta sheet content. The inhibition is likely due to attractive intermolecular interactions (hydrogen bonding) between menadione and lysozyme. Conclusions: In the present study, anti-amyloidogenic effect of menadione was evaluated on aggregation behaviour of human lysozyme which is responsible for systemic amyloidosis. These finding may provide new therapeutic approach to prevent systemic amyloidosis." @default.
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- W2479581917 date "2016-02-01" @default.
- W2479581917 modified "2023-09-29" @default.
- W2479581917 title "Menadione Suppresses Amyloid Fibrillogenesis and Cytotoxicity: Implication in the Treatment of Systemic Amyloidosis" @default.
- W2479581917 doi "https://doi.org/10.1016/j.bpj.2015.11.2852" @default.
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