Abstract Title:

Emodin inhibits aggregation of amyloid-β peptide 1-42 and improves cognitive deficits in Alzheimer's disease transgenic mice.

Abstract Source:

J Neurochem. 2020 Aug 16. Epub 2020 Aug 16. PMID: 32799401

Abstract Author(s):

Lichun Wang, Sitong Liu, Jiaqi Xu, Nobumoto Watanabe, Kevin H Mayo, Jiang Li, Xiaomeng Li

Article Affiliation:

Lichun Wang


Aggregation of amyloid-β peptide 1-42 (Aβ42) initiates the onset of Alzheimer's disease (AD), and all the drugs designed to attenuate AD have failed in clinical trials. Emodin reduces levels of β-amyloid, tau aggregation, oxidative stress, and inflammatory response, demonstrating AD therapeutic potential, whereas its effect on the accumulation of the amyloid-β protein is not well understood. In this work, we investigated emodin activity on Aβ aggregation using a range of biochemical, biophysical, and cell-based approaches. We provide evidence to suggest that emodin blocks Aβ42 fibrillogenesis and Aβ-induced cytotoxicity, displaying a greater effect than that of curcumin. Through adopting three short peptides (Aβ1-16, Aβ17-33, and Aβ28-42), it was proven that emodin interacts with the Leu17-Gly33 sequence. Furthermore, our findings indicated that Val18 and Phe19 in Aβ42 are the target residues with which emodin interacts according amino acid mutation experiments. When fed to 8-month-old B6C3-Tg mice for 2 months, high-dose emodin ameliorates cognitive impairment by 60%-70%. Pathological results revealed that levels of Aβ deposition in the brains of AD mice treated with a high dose of emodin decreased by 50%-70%. Therefore, our study indicates that emodin may represent a promising drug for AD treatment.

Study Type : Transgenic Animal Study

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