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Title 

BACE1 inhibition by genistein: biological evaluation, kinetic analysis, and molecular docking simulation

Authors 

K YounJ H ParkS LeeJinhyuk LeeE Y YunW S JeongM Jun

Publisher 

Mary Ann Liebert

Issue Date 

2018

Citation 

Journal of Medicinal Food

Keywords 

Alzheimer's diseasegenisteinin silico molecular dockingisoflavonesβ-secretase (BACE1)

Abstract 

β-site amyloid precursor protein cleaving enzyme 1 (BACE1) plays a role in generating amyloid β (Aβ), thus playing a major part early in the pathogenesis of Alzheimer's disease (AD). BACE1 has emerged as a crucial therapeutic target for decreasing the Aβ concentration in the AD brain. To explore natural BACE1 inhibitors, the present study concentrated on isoflavones, including genistein, formononetin, glycitein, daidzein, and puerarin. In this study, in vitro anti-AD activities were assessed using BACE1 inhibition assays, as well as enzyme kinetic predictions. Molecular docking analysis was applied to design potential BACE1 inhibitors. Among the major isoflavones, genistein exerted a notable BACE1 inhibition through reversible noncompetitive mechanism, while other compounds were less potent against BACE1. The docking study revealed that genistein had negative binding energy (-8.5 kcal/mol) and was stably positioned in the allosteric domains of BACE1 residues. It interacted with important amino acid residues in BACE1, such as ASN37, GLN73, and TRP76, through hydrogen bonding. The results suggested that genistein may be beneficial for preventing and/or treating AD. Furthermore, it may provide potential guidelines for the design of new BACE1 inhibitors

ISSN 

1096-620X

Link 

http://dx.doi.org/10.1089/jmf.2017.4068

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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