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• W4313245071 endingPage "109" @default.
• W4313245071 startingPage "109" @default.
• W4313245071 abstract "The deposition of β-amyloid (Aβ) in the brain leads to neurotoxic effects and subsequent Alzheimer's disease (AD). While AD is becoming more and more prevalent in modern society, therapeutic efforts targeting Aβ could be a promising solution. Currently, two natural products are reported to disintegrate preformed Aβ fibril in vitro. Meanwhile, the chemical driving force behind this phenomenon remains unknown. Taking cyanidin-3-O-glucoside (Cy-3G) as an example, here we studied its interaction with different Aβ polymorphs in silico. Negative charges on different Aβ polymorphs draw the interaction with the flavylium cation on Cy-3G. Our results show that Aβ in a single peptide form in solution exposed more hydrophobic solvent accessible surface area than its fibril structure (per protomer), and Cy-3G interacts more intensively with the single peptide form than fibril as indicated by more hydrogen bonding formed and more amino acid residues involved in their hydrophobic interactions. Thus, the single Aβ peptide aggregation into fibril and fibril dissociation into single peptide equilibrium could be disturbed by the preferential binding of Cy-3G to the monomeric Aβ peptide, which leads to the disassembly of the pathogenic Aβ fibril. This study offers a novel perspective of Cy-3G alleviated AD syndrome beyond its dogmatic antioxidant activity." @default.
• W4313245071 created "2023-01-06" @default.
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• W4313245071 date "2022-12-26" @default.
• W4313245071 modified "2023-10-14" @default.
• W4313245071 title "Molecular Mechanism of Cyanidin-3-O-Glucoside Disassembling Aβ Fibril In Silico" @default.
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• W4313245071 doi "https://doi.org/10.3390/nu15010109" @default.
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