jf304384b_si_001.pdf (197.45 kB)
α‑Glucosidase Inhibitors via Green Pathway: Biotransformation for Bicoumarins Catalyzed by Momordica charantia Peroxidase
journal contribution
posted on 2016-02-19, 22:06 authored by Xiao-Jun Hu, Xiao-Bing Wang, Ling-Yi KongPeroxidase 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.
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H 2O oxidativemultistep reactionsBicoumarins Catalyzedchiral compoundsinhibition dataglucosidaseresearchmethodGreen PathwayNoncompetitive binding modechiral biaryl axiscompounds 1Bioactive experimentsMomordica charantiabicoumarins 1Momordica charantia PeroxidasePeroxidaseantidiabetic agentsNMR spectroscopy
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