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

Abstract：

:The aggregation of α-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 α-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 α-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 α-synuclein tandem repeat (α-TR) in the aggregation process was studied.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Bae SY,Kim S,Hwang H,Kim HK,Yoon HC,Kim JH,Lee S,Kim TD

doi

10.1016/j.bbrc.2010.08.088

subject

Has Abstract

pub_date

2010-10-01 00:00:00

pages

531-6

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(10)01598-6

journal_volume

400

pub_type

杂志文章

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