24 365

Cited 23 times in

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

Authors
Bae, SY; Kim, S; Hwang, H; Kim, HK; Yoon, HC; Kim, JH; Lee, S; Kim, TD
Citation
Biochemical and biophysical research communications, 400(4):531-536, 2010
Journal Title
Biochemical and biophysical research communications
ISSN
0006-291X1090-2104
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.
MeSH terms
Amyloid/chemistry/*metabolismCatechin/analogs & derivatives/pharmacologyFlavanones/pharmacologyHumansImidazoles/*pharmacologyImides/*pharmacologyIonic Liquids/chemistryMicroscopy, Electron, TransmissionParkinson Disease/*metabolism*Tandem Repeat SequencesThiazoles/chemistryalpha-Synuclein/chemistry/*metabolism
DOI
10.1016/j.bbrc.2010.08.088
PMID
20801100
Appears in Collections:
Journal Papers > Research Organization > Chronic Inflammatory Disease Research Center
AJOU Authors
이, 상윤
Full Text Link
Export
RIS (EndNote)
XLS (Excel)
XML

qrcode

해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse