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Parkinson’s Disease
Volume 2010, Article ID 650794, 16 pages
Research Article

Effects of Various Flavonoids on the -Synuclein Fibrillation Process

1Department of Chemistry, University of California, Santa Cruz, CA 95064, USA
2Center for Computational Biology and Bioinformatics, Department of Biochemistry and Molecular Biology, Institute for Intrinsically Disordered Protein Research, Indiana University School of Medicine, 410 W. 10th Street, HS 5009, Indianapolis, IN 46202, USA
3Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow 142290, Russia

Received 26 May 2009; Revised 8 September 2009; Accepted 23 October 2009

Academic Editor: Mark Robert Cookson

Copyright © 2010 Xiaoyun Meng et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


-Synuclein aggregation and fibrillation are closely associated with the formation of Lewy bodies in neurons and are implicated in the causative pathogenesis of Parkinson's disease and other synucleinopathies. Currently, there is no approved therapeutic agent directed toward preventing the protein aggregation, which has been recently shown to have a key role in the cytotoxic nature of amyloidogenic proteins. Flavonoids, known as plant pigments, belong to a broad family of polyphenolic compounds. Over 4,000 flavonoids have been identified from various plants and foodstuffs derived from plants and have been demonstrated as potential neuroprotective agents. In this study 48 flavonoids belonging to several classes with structures differing in the position of double bonds and ring substituents were tested for their ability to inhibit the fibrillation of -synuclein in vitro. A variety of flavonoids inhibited -synuclein fibrillation, and most of the strong inhibitory flavonoids were also found to disaggregate preformed fibrils.