Abstract Title:

Silibinin inhibits acetylcholinesterase activity and amyloidβ peptide aggregation: a dual-target drug for the treatment of Alzheimer's disease.

Abstract Source:

Neurobiol Aging. 2015 Feb 11. Epub 2015 Feb 11. PMID: 25771396

Abstract Author(s):

Songwei Duan, Xiaoyin Guan, Runxuan Lin, Xincheng Liu, Ying Yan, Ruibang Lin, Tianqi Zhang, Xueman Chen, Jiaqi Huang, Xicui Sun, Qingqing Li, Shaoliang Fang, Jun Xu, Zhibin Yao, Huaiyu Gu

Article Affiliation:

Songwei Duan


Alzheimer's disease (AD) is characterized by amyloidβ (Aβ) peptide aggregation and cholinergic neurodegeneration. Therefore, in this paper, we examined silibinin, a flavonoid extracted from Silybum marianum, to determine its potential as a dual inhibitor of acetylcholinesterase (AChE) and Aβ peptide aggregation for AD treatment. To achieve this, we used molecular docking and molecular dynamics simulations to examine the affinity of silibinin with Aβ and AChE in silico. Next, we used circular dichroism and transmission electron microscopy to study the anti-Aβ aggregation capability of silibinin in vitro. Moreover, a Morris Water Maze test,enzyme-linked immunosorbent assay, immunohistochemistry, 5-bromo-2-deoxyuridine double labeling, and a gene gun experiment were performed on silibinin-treated APP/PS1 transgenic mice. In molecular dynamics simulations, silibinin interacted with Aβ and AChE to form different stable complexes. Afterthe administration of silibinin, AChE activity and Aβ aggregations were down-regulated, and the quantity of AChE also decreased. In addition, silibinin-treated APP/PS1 transgenic mice had greater scores in the Morris Water Maze. Moreover, silibinin could increase the number of newly generated microglia, astrocytes, neurons, and neuronal precursor cells. Taken together, these data suggest that silibinin could act as a dual inhibitor of AChE and Aβ peptide aggregation, therefore suggesting a therapeutic strategy for AD treatment.

Study Type : Transgenic Animal Study

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