金属-淀粉样蛋白-β的配位和聚集分析方法。

IF 2.9 3区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Metallomics Pub Date : 2023-01-10 DOI:10.1093/mtomcs/mfac102
Seongmin Park, Chanju Na, Jiyeon Han, Mi Hee Lim
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引用次数: 2

摘要

淀粉样蛋白-β (Aβ)肽的错误折叠和聚集是阿尔茨海默病(AD)患者大脑的组织病理学特征。为了发现AD的有效治疗方法,人们已经做出了许多努力来控制Aβ的聚集及其与其他病理因素(包括金属离子)的相互作用。金属离子,如Cu(II)和Zn(II),可以与Aβ肽结合形成金属结合的Aβ(金属-Aβ)复合物,并随后改变其聚集途径。特别是,氧化还原活性的金属离子结合到Aβ可以产生活性氧导致氧化应激。本文简要介绍了金属- α β配合物的配位和聚集特性的实验研究方法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Methods for analyzing the coordination and aggregation of metal-amyloid-β.

The misfolding and aggregation of amyloid-β (Aβ) peptides are histopathological features found in the brains of Alzheimer's disease (AD). To discover effective therapeutics for AD, numerous efforts have been made to control the aggregation of Aβ species and their interactions with other pathological factors, including metal ions. Metal ions, such as Cu(II) and Zn(II), can bind to Aβ peptides forming metal-bound Aβ (metal-Aβ) complexes and, subsequently, alter their aggregation pathways. In particular, redox-active metal ions bound to Aβ species can produce reactive oxygen species leading to oxidative stress. In this review, we briefly illustrate some experimental approaches for characterizing the coordination and aggregation properties of metal-Aβ complexes.

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来源期刊
Metallomics
Metallomics 生物-生化与分子生物学
CiteScore
7.00
自引率
5.90%
发文量
87
审稿时长
1 months
期刊介绍: Global approaches to metals in the biosciences
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