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The Identification of Biochanin A as a Potent and Selective β-Site App-Cleaving Enzyme 1 (Bace1) Inhibitor

by Kumju Youn 1,†, Ji-Hyun Park 1,†, Jinhyuk Lee 2,3, Woo-Sik Jeong 4,*, Chi-Tang Ho 5 and Mira Jun 1,6,*
Department of Food Science and Nutrition, Dong-A University, Busan 604-714, Korea
Korean Bioinformation Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea
Department of Bioinformatics, University of Sciences and Technology, Daejeon 305-350, Korea
Department of Food & Life Science, College of Biomedical Science & Engineering, Inje University, Gimhae 621-749, Korea
Department of Food Science, Rutgers University, New Brunswick, NJ 08901, USA
Institute of Convergence Bio-Health (ICBH), Dong-A University, 32, Daeshingongwon-Ro, Seo-Gu, Busan 602-715, Korea
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Nutrients 2016, 8(10), 637;
Received: 23 July 2016 / Revised: 1 October 2016 / Accepted: 10 October 2016 / Published: 14 October 2016
Beta-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the enzyme involved in the abnormal production of the amyloidogenic peptide Aβ, one of the major causes of histological hallmarks of Alzheimer’s disease (AD). Thus, BACE1 represents a key target protein in the development of new potential target for the prevention and treatment of AD. In this study, in vitro anti-AD activity of biochanin A, a dietary isoflavone found in legumes and most notably red clover, were evaluated via human recombinant BACE1 inhibition assay, as well as enzyme kinetic and molecular docking predictions. Enzyme-based assays revealed that biochanin A exhibited a non-competitive inhibitory effect on BACE1 with an IC50 value of 28 μM and a Ki of 43 μM. In addition, docking simulation results demonstrated that ASN37, SER35, SER36, TRP76, and ARG128 residues of BACE1 interacted with biochanin A. Moreover, the binding energy of biochanin A was negative (−8.4 kcal/mol), indicating that it might potentiate a strong binding between the compound and the allosteric site of BACE1, resulting in further effective BACE1 inhibition. The present novel findings raise the possibility that biochanin A may be used as a preventative, developed into a therapeutic agent for AD, or both. View Full-Text
Keywords: Alzheimer’s disease; β-secretase (BACE1); β-amyloid peptide (Aβ); biochanin A Alzheimer’s disease; β-secretase (BACE1); β-amyloid peptide (Aβ); biochanin A
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Youn, K.; Park, J.-H.; Lee, J.; Jeong, W.-S.; Ho, C.-T.; Jun, M. The Identification of Biochanin A as a Potent and Selective β-Site App-Cleaving Enzyme 1 (Bace1) Inhibitor. Nutrients 2016, 8, 637.

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