Alpha-glucosidase Inhibitory Mechanism of Phloridzin. | [Journal of Chemical Society of Pakistan • 2018]

Author(s):

1. Jiangwei Liu: School of Food Science, Henan Institute of Science and Technology, Xinxiang, China

2. Yuzhen Chen: School of Food Science, Henan Institute of Science and Technology, Xinxiang, China

3. Benguo Liu: School of Mathematical Sciences, Henan Institute of Science and Technology, Xinxiang, China

4. Guizhao Liang: Key Laboratory of Biorheological Science and Technology, Ministry of Education, School of Bioengineering, Chongqing University, Chongqing 400044, China

Abstract:

Summary: Phloridzin is a chalcone with potential application in functional food and medicine. In this study, the a-glucosidase inhibitory mechanism of phloridzin was investigated by inhibitory test, fluorescence spectroscopy and molecular docking method. The IC50 value of phloridzin was determined at 0.68 mmol/L. With the increase of phloridzin concentration, the static fluorescence quenching of a-glucosidase could be observed. The quenching constant (Kq), binding constant (KA) and the number of binding site (n) of phloridzin to a-glucosidase were 6.1474×1012, 1.3243×105 and 1.076, respectively. The molecular docking result suggested that phloridzin could play the inhibitory role by binding the Lys510 and Glu374 of a-glucosidase with hydrogen bonds.

Page(s): 799-803

DOI: DOI not available

Published: Journal: Journal of Chemical Society of Pakistan, Volume: 40, Issue: 4, Year: 2018

Keywords:

Keywords are not available for this article.

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