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Baicalein Inhibits Formation of α-Synuclein Oligomers within Living Cells and Prevents Aβ Peptide Fibrillation and Oligomerisation
Lu J.-H.2; Ardah M.T.1; Durairajan S.S.K.2; Liu L.-F.2; Xie L.-X.2; Fong W.-F.D.2; Hasan M.Y.1; Huang J.-D.3; El-Agnaf O.M.A.1; Li M.2
2011-03-07
Source PublicationChemBioChem
ISSN14394227 14397633
Volume12Issue:4Pages:615-624
AbstractAbnormal protein aggregation in the brain is linked to the pathogenesis of neurodegenerative diseases, including Alzheimer's disease (AD) and Parkinson's disease (PD). Recent studies revealed that the oligomeric form of aggregates is most likely the toxic species, and thus could be a good therapeutic target. To screen for potent inhibitors that can inhibit both oligomerisation and fibrillation of α-synuclein (α-syn), we systematically compared the antioligomeric and antifibrillar activities of eight compounds that were extracted from Chinese herbal medicines through three platforms that can monitor the formation of α-syn fibrils and oligomers in cell-free or cellular systems. Our results revealed that baicalein, a flavonoid extracted from the Chinese herbal medicine Scutellaria baicalensis Georgi ("huang qin" in Chinese), is a potent inhibitor of α-syn oligomerisation both in cell-free and cellular systems, and is also an effective inhibitor of α-syn fibrillation in cell-free systems. We further tested the protective effect of baicalein against α-syn-oligomer-induced toxicity in neuronal cells. Our data showed that baicalein inhibited the formation of α-syn oligomers in SH-SY5Y and Hela cells, and protected SH-SY5Y cells from α-syn-oligomer-induced toxicity. We also explored the effect of baicalein on amyloid-β peptide (Aβ) aggregation and toxicity. We found that baicalein can also inhibit Aβ fibrillation and oligomerisation, disaggregate pre-formed Aβ amyloid fibrils and prevent Aβ fibril-induced toxicity in PC12 cells. Our study indicates that baicalein is a good inhibitor of amyloid protein aggregation and toxicity. Given the role of these processes in neurodegenerative diseases such as AD and PD, our results suggest that baicalein has potential as a therapeutic agent for the treatment of these devastating disorders. Arrested aggregation: Baicalein, a flavonoid from the Chinese herbal medicine Scutellaria baicalensis Georgi, is a potent inhibitor of α-syn oligomerisation both in cell-free and cellular systems, and is also a effective inhibitor of α-syn fibrillation in cell-free systems. It inhibits the formation of α-syn oligomers in SH-SY5Y and Hela cells, and protects SH-SY5Y cells from α-syn-oligomer-induced toxicity. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
KeywordAlpha-synuclein Amyloid beta-peptides Baicalein Neurological agents Oligomerization
DOI10.1002/cbic.201000604
URLView the original
Language英語English
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Cited Times [WOS]:99   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionInstitute of Chinese Medical Sciences
Affiliation1.United Arab Emirates University
2.Hong Kong Baptist University
3.The University of Hong Kong Li Ka Shing Faculty of Medicine
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Lu J.-H.,Ardah M.T.,Durairajan S.S.K.,et al. Baicalein Inhibits Formation of α-Synuclein Oligomers within Living Cells and Prevents Aβ Peptide Fibrillation and Oligomerisation[J]. ChemBioChem,2011,12(4):615-624.
APA Lu J.-H.,Ardah M.T.,Durairajan S.S.K.,Liu L.-F.,Xie L.-X.,Fong W.-F.D.,Hasan M.Y.,Huang J.-D.,El-Agnaf O.M.A.,&Li M..(2011).Baicalein Inhibits Formation of α-Synuclein Oligomers within Living Cells and Prevents Aβ Peptide Fibrillation and Oligomerisation.ChemBioChem,12(4),615-624.
MLA Lu J.-H.,et al."Baicalein Inhibits Formation of α-Synuclein Oligomers within Living Cells and Prevents Aβ Peptide Fibrillation and Oligomerisation".ChemBioChem 12.4(2011):615-624.
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