| First Author | Wang L | Year | 2021 |
| Journal | J Neurochem | Volume | 157 |
| Issue | 6 | Pages | 1992-2007 |
| PubMed ID | 32799401 | Mgi Jnum | J:349384 |
| Mgi Id | MGI:6730214 | Doi | 10.1111/jnc.15156 |
| Citation | Wang L, et al. (2021) Emodin inhibits aggregation of amyloid-beta peptide 1-42 and improves cognitive deficits in Alzheimer's disease transgenic mice. J Neurochem 157(6):1992-2007 |
| abstractText | Aggregation of amyloid-beta peptide 1-42 (Abeta42) 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 beta-amyloid, tau aggregation, oxidative stress, and inflammatory response, demonstrating AD therapeutic potential, whereas its effect on the accumulation of the amyloid-beta protein is not well understood. In this work, we investigated emodin activity on Abeta aggregation using a range of biochemical, biophysical, and cell-based approaches. We provide evidence to suggest that emodin blocks Abeta42 fibrillogenesis and Abeta-induced cytotoxicity, displaying a greater effect than that of curcumin. Through adopting three short peptides (Abeta1-16, Abeta17-33, and Abeta28-42), it was proven that emodin interacts with the Leu17-Gly33 sequence. Furthermore, our findings indicated that Val18 and Phe19 in Abeta42 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 Abeta 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. |
