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利用固态圆二色光谱法研究蛋白质类淀粉样聚集体

Study of Protein Amyloid-Like Aggregates by Solid-State Circular Dichroism Spectroscopy.

作者信息

Hu Hong-Yu, Jiang Lei-Lei, Hong Jun-Ye

机构信息

Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences; 320 Yue-Yang Road, Shanghai 200031, China.

出版信息

Curr Protein Pept Sci. 2017;18(1):100-103. doi: 10.2174/1389203717666160709185323.

DOI:10.2174/1389203717666160709185323
PMID:27396751
Abstract

Protein aggregation and amyloidogenesis are closely associated with the pathogenesis of neurodegenerative diseases. Elucidating the morphology and structure of the amyloid aggregates or fibrils is important for understanding the molecular mechanisms of these proteinopathies. This review article describes the general principle and establishment of solid-state circular dichroism (ssCD) spectroscopy, and discusses its application for the analysis of secondary structures of proteins or peptides in amyloids and structural transformation of these proteins or peptides during their amyloidogenic aggregation.

摘要

蛋白质聚集和淀粉样蛋白形成与神经退行性疾病的发病机制密切相关。阐明淀粉样聚集体或纤维的形态和结构对于理解这些蛋白质病的分子机制很重要。这篇综述文章描述了固态圆二色光谱(ssCD)的一般原理和建立,并讨论了其在分析淀粉样蛋白中蛋白质或肽的二级结构以及这些蛋白质或肽在淀粉样蛋白生成聚集过程中的结构转变方面的应用。

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Structural and dynamic studies reveal that the Ala-rich region of ataxin-7 initiates α-helix formation of the polyQ tract but suppresses its aggregation.结构和动态研究揭示,ataxin-7 的富含丙氨酸区域启动了 polyQ 片段的 α-螺旋形成,但抑制了其聚集。
Sci Rep. 2019 May 16;9(1):7481. doi: 10.1038/s41598-019-43926-9.