Amyloid formation and disaggregation of α-synuclein and its tandem repeat (α-TR)
Amyloid formation and disaggregation of α-synuclein and its tandem repeat (α-TR)
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DOI：
10.1016/j.bbrc.2010.08.088
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发表时间：
2010-10-01
影响因子：
3.1
通讯作者：
Kim, T. Doohun
中科院分区：
文献类型：
--
作者：
Bae, Song Yi;Kim, Seulgi;Kim, T. Doohun
α-突触核蛋白的聚集与帕金森病的发病机制明显相关。因此，深入了解肌原纤维的形成机制，对临床治疗和诊断工具的发展具有重要意义。在这里，我们用几种生化技术，包括硫代黄素T分析和透射电子显微镜，研究了α-突触核蛋白与离子液体的相互作用。我们的数据表明，1-丁基-3-甲基咪唑双(三氟甲基磺酰基)亚胺[BIMbF(3)Im]能刺激α-突触核蛋白淀粉样纤维的快速形成，这些纤维可以被表没食子儿茶素没食子酸酯(EGCG)和黄芩素等多酚分解。此外，还研究了[BIMbF(3)Im]对聚集过程中α-突触核蛋白串联重复序列(α-tr)的影响。(C)2010 Elsevier Inc.保留所有权利。
The aggregation of alpha-synuclein is clearly related to the pathogenesis of Parkinson's disease. Therefore, detailed understanding of the mechanism of fibril formation is highly valuable for the development of clinical treatment and also of the diagnostic tools. Here, we have investigated the interaction of alpha-synuclein with ionic liquids by using several biochemical techniques including Thioflavin T assays and transmission electron microscopy (TEM). Our data shows a rapid formation of a-synuclein amyloid fibrils was stimulated by 1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide [BIMbF(3)Im], and these fibrils could be disaggregated by polyphenols such as epigallocatechin gallate (EGCG) and baicalein. Furthermore, the effect of [BIMbF(3)Im] on the alpha-synuclein tandem repeat (alpha-TR) in the aggregation process was studied. (C) 2010 Elsevier Inc. All rights reserved.