Journal
NUTRIENTS
Volume 8, Issue 10, Pages -Publisher
MDPI AG
DOI: 10.3390/nu8100637
Keywords
Alzheimer's disease; beta-secretase (BACE1); beta-amyloid peptide (A beta); biochanin A
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Funding
- Dong-A University
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Beta-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the enzyme involved inthe abnormal production of the amyloidogenic peptide A beta, 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 mu M and a Ki of 43 mu M. 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.
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