Title
α-Glucosidase Inhibitors via Green Pathway: Biotransformation for Bicoumarins Catalyzed by Momordica charantia Peroxidase
Author
Xiao-Jun Hu, Xiao-Bing Wang, Ling-Yi Kong
Year
2013
Journal
Journal of Agricultural and Food Chemistry
Abstract
Peroxidase extracted from Momordica charantia catalyzed the H2O2-dependent oxidative coupling of 7-hydroxy-4-methylcoumarin to form four new dimers (1–4) and two known ones (5,6). The structures, including the absolute configurations of axially chiral compounds, were unambiguously characterized by NMR spectroscopy, online HPLC-CD, and a variety of computational methods. Bioactive experiments demonstrated that compounds 1 and 2 had significant inhibitory effects on yeast α-glucosidase, much better than the controls. Noncompetitive binding mode was found by the graphical analysis of steady-state inhibition data. The mechanism of enzymatic inhibition confirmed in some depth that the inhibitors altered the secondary structure of α-glucosidase by decreasing the α-helix and increasing the β-sheet content. In summary, bicoumarins 1 and 2 might be exploited as the lead compounds for further research of antidiabetic agents, and this research provided a “green” method to synthesize compounds with the chiral biaryl axis generally calling for multistep reactions in organic chemistry.
Full Article
Instrument
J-810
Keywords
Circular dichroism, Absolute configuration, Agricultural and environmental, Secondary structure, Biochemistry