Au23(CR)14 nanocluster restores fibril Aβ’s unfolded state with abolished cytotoxicity and dissolves endogenous Aβ plaques
Abstract
The misfolding of amyloid-β (Aβ) peptides from the natural unfolded state to β-sheet structure is a critical step, leading to abnormal fibrillation and formation of endogenous Aβ plaques in Alzheimer's disease (AD). Previous studies have reported inhibition of Aβ fibrillation or disassembly of exogenous Aβ fibrils in vitro. However, soluble Aβ oligomers have been reported with increased cytotoxicity; this might partly explain why current...
Paper Details
Title
Au23(CR)14 nanocluster restores fibril Aβ’s unfolded state with abolished cytotoxicity and dissolves endogenous Aβ plaques
Published Date
Dec 20, 2019
Journal
Volume
7
Issue
4
Pages
763 - 774
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