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α-突触核蛋白 N 端的局部膜结合亲和力。

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

机构信息

Departments of Chemistry and Biology, Konstanz Research School Chemical Biology, 78457 Konstanz, Germany.

出版信息

Biochemistry. 2012 May 15;51(19):3960-2. doi: 10.1021/bi300357a. Epub 2012 Apr 30.

DOI:10.1021/bi300357a
PMID:22494024
Abstract

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.

摘要

α-突触核蛋白在路易体中大量存在，这是帕金森病的特征。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。电子顺磁共振波谱学与定点自旋标记相结合，允许对人工磷脂膜的蛋白-膜结合亲和力进行局部解析分析，并得到了对分离线粒体结合的研究支持。数据显示，N 端的结合亲和力是不均匀的。

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