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Bioassay-guided isolation of antioxidant and α-glucosidase inhibitory constituents from stem of Vigna angularis
[Display omitted] •Bioassay-guided isolation was performed to investigate the constituents in stem of Vigna angularis.•A new compound and a compound isolated from nature source firstly, along with 14 known compounds were isolated.•Most of the compounds shown significant α-glucosidase inhibitory acti...
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Published in: | Bioorganic chemistry 2019-06, Vol.87, p.312-320 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | [Display omitted]
•Bioassay-guided isolation was performed to investigate the constituents in stem of Vigna angularis.•A new compound and a compound isolated from nature source firstly, along with 14 known compounds were isolated.•Most of the compounds shown significant α-glucosidase inhibitory activity.•Enzyme kinetic analysis was conducted to determine type of inhibition and inhibition kinetic constant.
Stem of Vigna angularis (Willd.) Ohwi & H. Ohashi (VAS) is a main byproduct with considerable bioactivities. In present study, a bioassay-guided phytochemical investigation was used and led to the isolation of 16 compounds including one new compound (1) and one compound (2) isolated from nature source firstly along with 14 known compounds (3–16). The structures of isolates were identified by NMR and HR-ESI-MS data. The ability of antioxidant and α-glucosidase inhibition of the compounds were measured in vitro. Most of the ingredients shown strong ABTS radical scavenging activity (IC50 = 4.21–14.93 μM) and α-glucosidase inhibitory activity (IC50 = 0.05–34.14 μM). Enzyme kinetic analysis and molecular docking of compounds 1 and 2 were conducted. Compounds 1 and 2 were competitive inhibitor for α-glucosidase, with the inhibition kinetic constant value of 1.03 and 1.06 μM, respectively. The potent α-glucosidase inhibitory ability of compounds 1 and 2 resulted from firm binding with the active site of α-glucosidase. |
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ISSN: | 0045-2068 1090-2120 |
DOI: | 10.1016/j.bioorg.2019.03.041 |