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基底平面 HOPG 上淀粉样 β 肽聚集的直接电化学和 AFM 检测。

Direct electrochemical and AFM detection of amyloid-β peptide aggregation on basal plane HOPG.

机构信息

Interdisciplinary Nanoscience Center (iNANO), Science and Technology, Aarhus University, Gustav Wieds Vej 1590-14, DK-8000, Aarhus C, Denmark.

出版信息

Nanoscale. 2014 Jul 21;6(14):7853-7. doi: 10.1039/c4nr02413c.

DOI:10.1039/c4nr02413c
PMID:24934601
Abstract

Amyloidogenesis is associated with more than 30 human diseases, including Alzheimer's which is related to aggregation of β-amyloid peptide (Aβ). Here, consecutive stages of Aβ42 aggregation and amyloid fibril formation were followed electrochemically via oxidation of tyrosines in Aβ42 adsorbed on the basal plane graphite electrode and directly correlated with Aβ42 morphological changes observed by atomic force microscopy of the same substrate. The results offer new tools for analysis of mechanisms of Aβ aggregation.

摘要

淀粉样蛋白形成与超过 30 种人类疾病有关,包括与β-淀粉样肽(Aβ)聚集有关的阿尔茨海默病。在这里,通过吸附在基底平面石墨电极上的 Aβ42 中酪氨酸的氧化,电化学跟踪 Aβ42 聚集和淀粉样纤维形成的连续阶段,并与同一基底的原子力显微镜观察到的 Aβ42 形态变化直接相关。该结果为分析 Aβ 聚集机制提供了新的工具。

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