Probing amyloid protein aggregation with optical superresolution methods: from the test tube to models of disease

被引:36
|
作者
Kaminski, Clemens F. [1 ]
Schierle, Gabriele S. Kaminski [1 ]
机构
[1] Univ Cambridge, Dept Chem Engn & Biotechnol, Pembroke St, Cambridge CB2 3RA, England
基金
英国惠康基金; 英国工程与自然科学研究理事会; 英国医学研究理事会;
关键词
Alzheimer's disease; protein misfolding; superresolution microscopy; protein aggregation; INTRINSIC FLUORESCENCE; BETA; MECHANISMS; SIGNATURE; OLIGOMERS; TOXICITY; TAU;
D O I
10.1117/1.NPh.3.4.041807
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The misfolding and self-assembly of intrinsically disordered proteins into insoluble amyloid structures are central to many neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. Optical imaging of this self-assembly process in vitro and in cells is revolutionizing our understanding of the molecular mechanisms behind these devastating conditions. In contrast to conventional biophysical methods, optical imaging and, in particular, optical superresolution imaging, permits the dynamic investigation of the molecular self-assembly process in vitro and in cells, at molecular-level resolution. In this article, current state-of-the-art imaging methods are reviewed and discussed in the context of research into neurodegeneration. (C) The Authors. Published by SPIE under a Creative Commons Attribution 3.0 Unported License. Distribution or reproduction of this work in whole or in part requires full attribution of the original publication, including its DOI.
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页数:9
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