Properties of native brain α-synuclein.
Properties of native brain α-synuclein.
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由T. Bartels，J. G. Choi & D. J·塞尔科10.1038/nature 10324 α-突触核蛋白是一种丰富的突触前蛋白，其结合带负电荷的磷脂，作为SNARE复合物伴侣蛋白发挥作用，并有助于帕金森病的发病机制。重组α-突触核蛋白在溶液中大部分是未折叠的，缺乏三级结构，，但Bartelset等人提出，从人红细胞中纯化的天然α-突触核蛋白形成稳定折叠的可溶性四聚体，可抵抗聚集。相比之下，我们在这里表明，从小鼠脑中纯化的天然α-突触核蛋白主要由非结构化单体组成，没有稳定的四聚体形成，并且易于聚集。α-突触核蛋白的天然状态对于理解其病理作用是重要的，因为稳定折叠的蛋白质比构象不稳定的蛋白质更不容易聚集。有一个答复这个简短的通信产生的巴特尔斯，T。& Selkoe，D. J.Nature498，http://dx.doi.org/10.1038/nature12126（2013）.
Arising fromT. Bartels, J. G. Choi & D. J. Selkoe. Nature477, 107–110 (2011).10.1038/nature10324α-Synuclein is an abundant presynaptic protein that binds to negatively charged phospholipids,, functions as a SNARE-complex chaperone and contributes to Parkinson’s disease pathogenesis,. Recombinant α-synuclein in solution is largely unfolded and devoid of tertiary structure,,,,,, but Bartelset al.have proposed that native α-synuclein purified from human erythrocytes forms a stably folded, soluble tetramer that resists aggregation. By contrast, we show here that native α-synuclein purified from mouse brain consists of a largely unstructured monomer, exhibits no stable tetramer formation, and is prone to aggregation. The native state of α-synuclein is important for understanding its pathological effects as a stably folded protein would be much less prone to aggregation than a conformationally labile protein. There is a Reply to this Brief Communication Arising by Bartels, T. & Selkoe, D. J.Nature498, http://dx.doi.org/10.1038/nature12126 (2013).