Amyloid formation and disaggregation of α-synuclein and its tandem repeat (α-TR)

被引：28
|
作者：
Bae, Song Yi [2 ]
Kim, Seulgi [2 ]
Hwang, Heejin [2 ]
Kim, Hyun-Kyung [2 ]
Yoon, Hyun C. [2 ]
Kim, Jae Ho [2 ]
Lee, SangYoon [1 ]
Kim, T. Doohun [2 ]
机构：
[1] Ajou Univ, Chron Inflammatory Dis Res Ctr, Sch Med, Suwon 443749, South Korea
[2] Ajou Univ, Dept Mol Sci & Technol, Grad Sch Interdisciplinary Programs, Suwon 443749, South Korea
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2010年 / 400卷 / 04期
关键词：
alpha-Synuclein; Amyloid fibrils; Parkinson's disease (PD); Ionic liquids (ILs); AGGREGATION;
D O I：
10.1016/j.bbrc.2010.08.088
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：531 / 536
页数：6
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