肽
伴侣(临床)
化学
纳米材料
蛋白质折叠
生物物理学
纳米技术
淀粉样纤维
限制
生物化学
材料科学
淀粉样β
生物
医学
机械工程
疾病
病理
工程类
作者
Guanbin Gao,Xinglin Liu,Zhenhua Gu,Qingxue Mu,Guowei Zhu,Ting Zhang,Cheng Zhang,Ling Zhou,Lei Shen,Taolei Sun
出处
期刊:Nano Letters
[American Chemical Society]
日期:2022-03-17
卷期号:22 (7): 2964-2970
被引量:5
标识
DOI:10.1021/acs.nanolett.2c00149
摘要
Synthetic nanomaterials possessing biomolecular-chaperone functions are good candidates for modulating physicochemical interactions in many bioapplications. Despite extensive research, no general principle to engineer nanomaterial surfaces is available to precisely manipulate biomolecular conformations and behaviors, greatly limiting attempts to develop high-performance nanochaperone materials. Here, we demonstrate that, by quantifying the length (-SCxR±, x = 3-11) and charges (R- = -COO-, R+ = -NH3+) of ligands on Au25 gold nanochaperones (AuNCs), simulating binding sites and affinities of amyloid-like peptides with AuNCs, and probing peptide folding and fibrillation in the presence of AuNCs, it is possible to precisely manipulate the peptides' conformations and, thus, their amyloidosis via customizing AuNCs nanointerfaces. We show that intermediate-length liganded AuNCs with a specific charge chaperone peptides' native conformations and thus inhibit their fibrillation, while other types of AuNCs destabilize peptides and promote their fibrillation. We offer a microscopic molecular insight into peptide identity on AuNCs and provide a guideline in customizing nanochaperones via manipulating their nanointerfaces.
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