α-突触核蛋白的功能和失活：通过单分子荧光探测构象变化和聚集。
Function and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescence.
机构信息
Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, P.O. Box 208114, New Haven, CT 06511, USA.
出版信息
Mol Neurobiol. 2013 Apr;47(2):622-31. doi: 10.1007/s12035-012-8338-x. Epub 2012 Sep 16.
Abstract
The aggregation and deposition of the neuronal protein α-synuclein in the substantia nigra region of the brain is a key pathological feature of Parkinson's disease. α-Synuclein assembles from a monomeric state in solution, which lacks stable secondary and tertiary contacts, into highly structured fibrillar aggregates through a pathway which involves the population of multiple oligomeric species over a range of time scales. These features make α-synuclein well suited for study with single-molecule techniques, which are particularly useful for characterizing dynamic, heterogeneous samples. Here, we review the current literature featuring single-molecule fluorescence studies of α-synuclein and discuss how these studies have contributed to our understanding of both its function and its role in disease.
摘要
神经元蛋白α-突触核蛋白在大脑黑质区域的聚集和沉积是帕金森病的一个关键病理特征。α-突触核蛋白从溶液中的单体状态组装而成，缺乏稳定的二级和三级接触，通过一个途径形成高度结构化的纤维状聚集物，该途径涉及多种低聚物物种在一系列时间尺度上的出现。这些特性使 α-突触核蛋白非常适合使用单分子技术进行研究，单分子技术对于表征动态、异质的样品特别有用。在这里，我们回顾了单分子荧光研究 α-突触核蛋白的现有文献，并讨论了这些研究如何促进我们对其功能及其在疾病中的作用的理解。
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