Silibinin: A novel inhibitor of Aβ aggregation

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DOIResolve DOI: http://doi.org/10.1016/j.neuint.2010.12.017
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TypeArticle
Journal titleNeurochemistry International
Volume58
Issue3
Pages399403; # of pages: 5
SubjectAβ aggregation; Neurotoxicity; Silibinin; Thioflavin T (ThT) assay aggregation; Neurotoxicity; Silibinin; Thioflavin T (ThT) assay
AbstractAlzheimer's disease (AD) is characterized by the abnormal aggregation of amyloid β peptide (Aβ) into extracellular fibrillar deposits known as amyloid plaque. Inhibition of Aβ aggregation is therefore viewed as a potential method to halt or slow the progression of AD. It is reported that silibinin (silybin), a flavonoid derived from the herb milk thistle (Silybum marianum), attenuates cognitive deficits induced by Aβ25-35 peptide and methamphetamine. However, it remains unclear whether silibinin interacts with Aβ peptide directly and decreases Aβ peptide-induced neurotoxicity. In the present study, we identified, through employing a ThT assay and electron microscopic imaging that silibinin also appears to act as a novel inhibitor of Aβ aggregation and this effect showed dose-dependency. We also show that silibinin prevented SH-SY5Y cells from injuries caused by Aβ1-42-induced oxidative stress by decreasing H2O2 production in Aβ1-42-stressed neurons. Taken together, these results indicate that silibinin may be a novel therapeutic agent for the treatment of AD.
Publication date
LanguageEnglish
AffiliationNRC Institute for Nutrisciences and Health; National Research Council Canada
Peer reviewedYes
NPARC number17364201
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Record identifier80200306-166b-42ee-898c-1d0591c00cb9
Record created2011-03-22
Record modified2016-05-09
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