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AuthorArdah, Mustafa T.
AuthorPaleologou, Katerina E.
AuthorLv, Guohua
AuthorMenon, Sindhu A.
AuthorAbul Khair, Salema B.
AuthorLu, Jia-Hong
AuthorSafieh-Garabedian, Bared
AuthorAl-Hayani, Abdulmonem A.
AuthorEliezer, David
AuthorLi, Min
AuthorEl-Agnaf, Omar M.A.
Available date2016-11-22T06:39:03Z
Publication Date2015-02-01
Publication NameNeurobiology of Diseaseen_US
CitationMustafa T. Ardah, Katerina E. Paleologou, Guohua Lv, Sindhu A. Menon, Salema B. Abul Khair, Jia-Hong Lu, Bared Safieh-Garabedian, Abdulmonem A. Al-Hayani, David Eliezer, Min Li, Omar M.A. El-Agnaf, Ginsenoside Rb1 inhibits fibrillation and toxicity of alpha-synuclein and disaggregates preformed fibrils, Neurobiology of Disease, Volume 74, February 2015, Pages 89-101
AbstractCompelling evidence indicates that α-synuclein (α-syn) aggregation plays a central role in the pathogenesis of Parkinson's disease (PD) and other synucleinopathies. Identification of compounds that inhibit or reverse the aggregation process may thus represent a viable therapeutic strategy against PD and related disorders. Ginseng is a well-known medicinal plant that has been used in East Asia for more than two thousand years to treat several conditions. It is now understood that the pharmacological properties of ginseng can be attributed to its biologically active components, the ginsenosides, which in turn have been shown to have neuroprotective properties. We therefore sought to determine for the first time, the potential of the most frequently used and studied ginsenosides, namely Rg1, Rg3 and Rb1, as anti-amyloidogenic agents. The effect of Rg1, Rg3 and Rb1 on α-syn aggregation and toxicity was determined by an array of biophysical, biochemical and cell-culture-based techniques. Among the screened ginsenosides, only Rb1 was shown to be a potent inhibitor of α-syn fibrillation and toxicity. Additionally, Rb1 exhibited a strong ability to disaggregate preformed fibrils and to inhibit the seeded polymerization of α-syn. Interestingly, Rb1 was found to stabilize soluble non-toxic oligomers with no β-sheet content, that were susceptible to proteinase K digestion, and the binding of Rb1 to those oligomers may represent a potential mechanism of action. Thus, Rb1 could represent the starting point for designing new molecules that could be utilized as drugs for the treatment of PD and related disorders.
SponsorSheikh Hamdan Bin Rashid Al Maktoum Award for Medical Sciences (Dubai, UAE; Grant MRG-23/2005–2006). This study was made possible by NPRP grant 4-1371-1-223 from the Qatar National Research Fund (a member of Qatar Foundation). DE is also supported by NIH/NIA grant AG019391. MA was supported by United Arab Emirates University — PhD scholarship.
SubjectParkinson's disease
SubjectAmyloid fibrils
SubjectDrug discovery
TitleGinsenoside Rb1 inhibits fibrillation and toxicity of alpha-synuclein and disaggregates preformed fibrils
Volume Number74

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