Locally resolved membrane binding affinity of the N-terminus of α-synuclein.

Locally resolved membrane binding affinity of the N-terminus of α-synuclein.
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α-突触核蛋白 N 末端的局部解析膜结合亲和力

DOI:
10.1021/bi300357a
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发表时间:
2012
期刊:
影响因子:
2.9
通讯作者:
Drescher M
Drescher M
中科院分区:
生物学3区
文献类型:
--
作者:
Robotta M;Hintze C;Schildknecht S;Zijlstra N;Jüngst C;Karreman C;Huber M;Leist M;Subramaniam V;Drescher M

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α-突触核蛋白大量存在于路易体中,是帕金森病的特征。其确切的生理作用尚未确定,但线粒体膜结合被怀疑是其功能的一个关键方面。电子顺磁共振光谱结合定点自旋标记允许人工磷脂膜的蛋白质-膜结合亲和力的局部解析分析,支持的结合分离的线粒体的研究。数据显示N-末端的结合亲和力是不均匀的。
α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson’s disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein–membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform.
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