Department of Chemistry, Zukunftskolleg, and Konstanz Research School Chemical Biology, University of Konstanz , 78457 Konstanz, Germany.
Department of Physics, State University of Londrina , 86057-970 Londrina, Brazil.
J Am Chem Soc. 2017 Mar 29;139(12):4254-4257. doi: 10.1021/jacs.6b05335. Epub 2017 Mar 20.
The intrinsically disordered human protein alpha-Synuclein (αS) has a prominent role in Parkinson's disease (PD) pathology. Several familial variants of αS are correlated with inherited PD. Disease mutations have been shown to have an impact on lipid membrane binding. Here, using electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling, we show that familial PD-associated variants are structurally defective in membrane binding and alter the local binding properties of the protein.
人类无规则蛋白α-突触核蛋白（αS）在帕金森病（PD）的病理中起着重要作用。几种家族性αS 变体与遗传性 PD 相关。研究表明，疾病突变会影响脂质膜结合。在这里，我们使用电子顺磁共振波谱学结合定点自旋标记技术，表明与家族性 PD 相关的变体在膜结合方面存在结构缺陷，并改变了蛋白质的局部结合特性。
