Neuropathology, biochemistry, and biophysics of a-synuclein aggregation

                 a-synuclein聚集的神经病理学、生物化学和生理学  

Abstract

Aggregation of a-synuclein, an abundant and conserved presynaptic brain protein, is implicated as a critical factor in several neurodegenerative diseases}. These diseases, known as synucleinopathies, include Parkinson’s disease, dementia with Lewy bodies (LBs), diffuse LB disease, the LB variant of Alzheimer’s disease, multiple system atrophy, and neurodegeneration with brain iron accumulation type.Although the precise nature of in vivo a-synuclein function remains elusive, considerable knowledge has been accumulated about its structural properties and conformational behavior.a-Synuclein is a typical natively unfolded protein.  It is characterized by the lack of rigid, well-defined, 3-D structure and possesses remarkable conformational plasticity.The structure of this protein depends dramatically on its environment and it accommodates a number of unrelated conformations. This paper provides an overview of the biochemistry, biophysics, and neuropathology of a-synuclein aggregation.

     a-synuclein (丰富和保守的突触前的脑蛋白)的聚集是涉及许多神经变性疾病关键因素。这些被称为synuclein病理的疾病包括帕金森病、Lewy体(LBs )痴呆、散发LB 病、LB 突变的阿尔茨海默病、多系统萎缩症和I型伴脑组织铁离子蓄积的神经变性病。功能的准确特性仍然不明，但已经越来越多地认识到了它的结构特征和构象性能。a-Synuclein 是一个典型自然展开的蛋白，它以缺乏硬度、容易辨认、3-D结构并且具有显著的构象可塑性为特征，蛋白结构明显依赖它的环境并且含有许多无关的结构。此论文提供a-synuclein 聚集的生物化学、生理学和神经病理学概观。

Keywords: aggregation, fibril, natively unfolded protein, neurodegeneration, synucleinopathies, a-synuclein.