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Au(23)(CR)(14) nanocluster restores fibril Aβ’s unfolded state with abolished cytotoxicity and dissolves endogenous Aβ plaques

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...

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Detalles Bibliográficos
Autores principales: Zhang, Wenkang, Gao, Guanbin, Ma, Zhongjie, Luo, Zhuoying, He, Meng, Sun, Taolei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8289031/
https://www.ncbi.nlm.nih.gov/pubmed/34692095
http://dx.doi.org/10.1093/nsr/nwz215

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