51. Isolation and identification of α-glucosidase inhibitory constituents from the seeds of Vigna nakashimae: Enzyme kinetic study with active phytochemical
- Author
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Seok Bo Song, Myeong-Eun Choe, Jin Hwan Lee, Jong-Min Ko, Jee-Yeon Ko, Chang-Hwan Park, Tae Joung Ha, and Do-Yeon Kwak
- Subjects
0301 basic medicine ,Magnetic Resonance Spectroscopy ,Phytochemicals ,Molecular Conformation ,Saccharomyces cerevisiae ,Fractionation ,Food chemistry ,Catechin ,Analytical Chemistry ,Vigna ,Inhibitory Concentration 50 ,03 medical and health sciences ,0404 agricultural biotechnology ,Phenols ,Glycoside Hydrolase Inhibitors ,IC50 ,chemistry.chemical_classification ,Aldose reductase ,Chromatography ,biology ,Plant Extracts ,Chemistry ,alpha-Glucosidases ,04 agricultural and veterinary sciences ,General Medicine ,biology.organism_classification ,040401 food science ,Kinetics ,030104 developmental biology ,Enzyme ,Phytochemical ,Alpha-glucosidase ,Seeds ,biology.protein ,Food Science - Abstract
The α-glucosidase inhibition effects of the 80% ethanol extracts in the seeds of five Vigna species (V. nakashimae, V. nipponensis, V. umbellate, V. radiate, and V. angularis) were evaluated and their half-maximal inhibitory concentration (IC50) values showed considerable differences (p 900 μg/ml. V. nakashimae exhibited the most potent inhibition with IC50 value of 7.3 ± 1.1 μg/ml, followed by V. nipponensis (184.0 ± 9.5 μg/ml) and V. umbellata (520.0 ± 8.1 μg/ml). Bioactivity-guided fractionation of V. nakashimae seeds yielded three phenolics by silica gel chromatography and their structures were elucidated as gambiriin D (1), luteoliflavan-7-O-glucopyranoside (2), and catechin-7-O-glucopyranoside (3) using nuclear magnetic resonance (NMR) spectroscopy. In particular, gambiriin D (1) possessed strong inhibition activity with IC50 of 36.8 ± 2.3 μM through simple reversible slow-binding inhibition (kinetic parameters: k4 = 0.0048 μM−1s−1; Kiapp = 48 μM). Furthermore, this compound inhibited recombinant human aldose reductase with IC50 value of 12.0 ± 0.7 μM. Results suggest that V. nakashimae may be a potent α-glucosidase inhibition for health products.
- Published
- 2018
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