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Issue 52, 2017, Issue in Progress
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(−)-Epigallocatechin-3-gallate (EGCG) inhibits fibrillation, disaggregates amyloid fibrils of α-synuclein, and protects PC12 cells against α-synuclein-induced toxicity

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Abstract

α-Synuclein (α-Syn) aggregates are the major component of Lewy bodies (LB), which is a pathological hallmark in the brain tissue of Parkinson's disease (PD) patients. It has been reported that (−)-epigallocatechin-3-gallate (EGCG) is biologically able to penetrate the blood–brain barrier and inhibit the fibrillation of amyloid proteins. This study aimed to provide insight into the possible mechanism of EGCG as a potential candidate agent for the prevention and treatment of PD on the basis of the interaction between α-Syn and EGCG. In the present study, the effects of EGCG on the fibrillation and disaggregation of α-Syn were investigated by thioflavin T (ThT) fluorescence spectroscopy, circular dichroism spectroscopy (CD), nuclear magnetic resonance (NMR) spectroscopy, atomic force microscopy (AFM) and transmission electron microscopy (TEM) on a molecular level. In addition, on the cellular level, we investigated the protective effects of EGCG on α-Syn-induced cell death in the transduced PC12 cells which overexpressed α-Syn, using the techniques of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay, 2,7-dichlorodihydrofluorescein diacetate (DCFH-DA) assay, western blot and confocal laser scanning microscopy. It was found that EGCG not only significantly inhibited the conformational transition of α-Syn from random coil to β-sheet conformers through binding to Ile, Phe and Tyr amino residues, but also disaggregated the amyloid fibrils of α-Syn in a dose-dependent manner, through binding to Leu, His, Phe and Tyr amino residues. It is also demonstrated that EGCG can protect PC12 cells against α-Syn-induced damage by inhibiting the overexpression and fibrillation of α-Syn in the cells.

Graphical abstract: (−)-Epigallocatechin-3-gallate (EGCG) inhibits fibrillation, disaggregates amyloid fibrils of α-synuclein, and protects PC12 cells against α-synuclein-induced toxicity

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Publication details

The article was received on 01 Apr 2017, accepted on 20 Jun 2017 and first published on 26 Jun 2017


Article type: Paper
DOI: 10.1039/C7RA03752J
Citation: RSC Adv., 2017,7, 32508-32517
  • Open access: Creative Commons BY-NC license
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    (−)-Epigallocatechin-3-gallate (EGCG) inhibits fibrillation, disaggregates amyloid fibrils of α-synuclein, and protects PC12 cells against α-synuclein-induced toxicity

    J. Zhao, Q. Liang, Q. Sun, C. Chen, L. Xu, Y. Ding and P. Zhou, RSC Adv., 2017, 7, 32508
    DOI: 10.1039/C7RA03752J

    This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

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      [Original citation] - Published by The Royal Society of Chemistry.

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