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Title: Amyloid formation and disaggregation of {alpha}-synuclein and its tandem repeat ({alpha}-TR)

Abstract

Research highlights: {yields} Formation of the {alpha}-synuclein amyloid fibrils by [BIMbF{sub 3}Im]. {yields} Disaggregation of amyloid fibrils by epigallocatechin gallate (EGCG) and baicalein. {yields} Amyloid formation of {alpha}-synuclein tandem repeat ({alpha}-TR). -- Abstract: 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 {alpha}-synuclein amyloid fibrils was stimulated by 1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide [BIMbF{sub 3}Im], and these fibrils could be disaggregated by polyphenols such as epigallocatechin gallate (EGCG) and baicalein. Furthermore, the effect of [BIMbF{sub 3}Im] on the {alpha}-synuclein tandem repeat ({alpha}-TR) in the aggregation process was studied.

Authors:
; ; ; ; ;  [1];  [2]
  1. Department of Molecular Science and Technology, Graduate School of Interdisciplinary Programs, Ajou University, Suwon 443-749 (Korea, Republic of)
  2. Chronic Inflammatory Disease Research Center, School of Medicine, Ajou University, Suwon 443-749 (Korea, Republic of)
Publication Date:
OSTI Identifier:
22202787
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 400; Journal Issue: 4; Other Information: Copyright (c) 2010 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; 60 APPLIED LIFE SCIENCES; AGGLOMERATION; MOLTEN SALTS; NERVOUS SYSTEM DISEASES; PATHOGENESIS; POLYPHENOLS; TRANSMISSION ELECTRON MICROSCOPY

Citation Formats

Bae, Song Yi, Kim, Seulgi, Hwang, Heejin, Kim, Hyun-Kyung, Yoon, Hyun C., Kim, Jae Ho, Lee, SangYoon, and Kim, T. Doohun, E-mail: doohunkim@ajou.ac.kr. Amyloid formation and disaggregation of {alpha}-synuclein and its tandem repeat ({alpha}-TR). United States: N. p., 2010. Web. doi:10.1016/J.BBRC.2010.08.088.
Bae, Song Yi, Kim, Seulgi, Hwang, Heejin, Kim, Hyun-Kyung, Yoon, Hyun C., Kim, Jae Ho, Lee, SangYoon, & Kim, T. Doohun, E-mail: doohunkim@ajou.ac.kr. Amyloid formation and disaggregation of {alpha}-synuclein and its tandem repeat ({alpha}-TR). United States. https://doi.org/10.1016/J.BBRC.2010.08.088
Bae, Song Yi, Kim, Seulgi, Hwang, Heejin, Kim, Hyun-Kyung, Yoon, Hyun C., Kim, Jae Ho, Lee, SangYoon, and Kim, T. Doohun, E-mail: doohunkim@ajou.ac.kr. 2010. "Amyloid formation and disaggregation of {alpha}-synuclein and its tandem repeat ({alpha}-TR)". United States. https://doi.org/10.1016/J.BBRC.2010.08.088.
@article{osti_22202787,
title = {Amyloid formation and disaggregation of {alpha}-synuclein and its tandem repeat ({alpha}-TR)},
author = {Bae, Song Yi and Kim, Seulgi and Hwang, Heejin and Kim, Hyun-Kyung and Yoon, Hyun C. and Kim, Jae Ho and Lee, SangYoon and Kim, T. Doohun, E-mail: doohunkim@ajou.ac.kr},
abstractNote = {Research highlights: {yields} Formation of the {alpha}-synuclein amyloid fibrils by [BIMbF{sub 3}Im]. {yields} Disaggregation of amyloid fibrils by epigallocatechin gallate (EGCG) and baicalein. {yields} Amyloid formation of {alpha}-synuclein tandem repeat ({alpha}-TR). -- Abstract: 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 {alpha}-synuclein amyloid fibrils was stimulated by 1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide [BIMbF{sub 3}Im], and these fibrils could be disaggregated by polyphenols such as epigallocatechin gallate (EGCG) and baicalein. Furthermore, the effect of [BIMbF{sub 3}Im] on the {alpha}-synuclein tandem repeat ({alpha}-TR) in the aggregation process was studied.},
doi = {10.1016/J.BBRC.2010.08.088},
url = {https://www.osti.gov/biblio/22202787}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 4,
volume = 400,
place = {United States},
year = {Fri Oct 01 00:00:00 EDT 2010},
month = {Fri Oct 01 00:00:00 EDT 2010}
}