A small-angle X-ray scattering study of alpha-synuclein from human red blood cells.
A small-angle X-ray scattering study of alpha-synuclein from human red blood cells.
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DOI：
10.1038/srep30473
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发表时间：
2016-07-29
影响因子：
4.6
通讯作者：
Mochizuki H
中科院分区：
文献类型：
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作者：
Araki K;Yagi N;Nakatani R;Sekiguchi H;So M;Yagi H;Ohta N;Nagai Y;Goto Y;Mochizuki H
α-突触核蛋白（α-syn）是路易体的主要成分，路易体是帕金森病患者的神经病理学标志。由于人红细胞α-syn在生理条件下是否以四聚体形式存在一直存在争议，我们尝试用小角X射线溶液散射方法解决这一问题。在两种不同的条件下（使用Tris缓冲液的高离子强度和使用乙酸铵缓冲液的低离子强度），未发现存在四聚体的证据。当比较红细胞和重组α-syn分子时，我们发现尽管缓冲条件强烈影响蛋白质的回转半径，但分子量和二级结构没有显著差异。结果表明，尽管α-syn不能形成稳定的四聚体，但其构象与所处的环境密切相关，这可能是其在细胞内易于聚集的原因。
α-synuclein (α-syn) is the main component of Lewy bodies, which are neuropathological hallmarks of patients with Parkinson’s disease. As it has been controversial whether human α-syn from erythrocytes exists as a tetramer under physiological conditions, we tried solving this issue by the small-angle X-ray solution scattering method. Under two different conditions (high ionic strength with a Tris buffer and low ionic strength with an ammonium acetate buffer), no evidence was found for the presence of tetramer. When comparing erythrocyte and recombinant α-syn molecules, we found no significant difference of the molecular weight and the secondary structure although the buffer conditions strongly affect the radius of gyration of the protein. The results indicate that, even though a stable tetramer may not be formed, conformation of α-syn depends much on its environment, which may be the reason for its tendency to aggregate in cells.