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Abstract Title:

Biological and Computational Studies for Dual Cholinesterases Inhibitory Effect of Zerumbone.

Abstract Source:

Nutrients. 2020 Apr 25 ;12(5). Epub 2020 Apr 25. PMID: 32344943

Abstract Author(s):

Jayeong Hwang, Kumju Youn, Yeongseon Ji, Seonah Lee, Gyutae Lim, Jinhyuk Lee, Chi-Tang Ho, Sun-Hee Leem, Mira Jun

Article Affiliation:

Jayeong Hwang

Abstract:

Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) mediate the degradation of acetylcholine (ACh), a primary neurotransmitter in the brain. Cholinergic deficiency occurs during the progression of Alzheimer's disease (AD), resulting in widespread cognitive dysfunction and decline. We evaluated the potential effect of a natural cholinesterase inhibitor, zerumbone, using in vitro target enzyme assays, as well as in silico docking and ADMET (absorption, distribution, metabolism, excretion, and toxicity) simulation. Zerumbone showed a predominant cholinesterase inhibitory property with ICvalues of 2.74± 0.48 µM and 4.12 ± 0.42 µM for AChE and BChE, respectively; however, the modes of inhibition were different. Computational docking simulation indicated that Van der Waals interactions between zerumbone and both the cholinesterases were the main forces responsible for its inhibitory effects. Furthermore, zerumbone showed the best physicochemical properties for both bioavailability and blood-brain barrier (BBB) permeability. Together, in the present study, zerumbone was clearly identified as a unique dual AChE and BChE inhibitor with high permeability across the BBB, suggesting a strong potential for its physiological benefits and/or pharmacological efficacy in the prevention of AD.

Study Type : In Vitro Study

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