α-Glucosidase Inhibitory Mechanism of Phloridzin

被引：0
|
作者：
Liu, Jiangwei [1 ]
Chen, Yuzhen [2 ]
Liu, Benguo [1 ]
Liang, Guizhao [3 ]
机构：
[1] Henan Inst Sci & Technol, Sch Food Sci, Xinxiang 453003, Peoples R China
[2] Henan Inst Sci & Technol, Sch Math Sci, Xinxiang 453003, Peoples R China
[3] Chongqing Univ, Sch Bioengn, Key Lab Biorheol Sci & Technol, Minist Educ, Chongqing 400044, Peoples R China
来源：
JOURNAL OF THE CHEMICAL SOCIETY OF PAKISTAN | 2018年 / 40卷 / 04期
基金：
中国国家自然科学基金;
关键词：
Phloridzin; alpha-Glucosidase; Inhibitory mechanism; Fluorescence spectroscopy; Molecular docking; MOLECULAR DOCKING; FLAVONOIDS; IDENTIFICATION; ANTIOXIDANT; DERIVATIVES; AMYLASE; 3D-QSAR; TRYPSIN; SEARCH;
D O I：
暂无
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Phloridzin is a chalcone with potential application in functional food and medicine. In this study, the alpha-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 alpha-glucosidase could be observed. The quenching constant (Kq), binding constant (K-A) and the number of binding site (n) of phloridzin to alpha-glucosidase were 6.1474x10(12), 1.3243X10(5) and 1.076, respectively. The molecular docking result suggested that phloridzin could play the inhibitory role by binding the Lys510 and G1u374 of alpha-glucosidase with hydrogen bonds.
引用
收藏
页码：799 / 803
页数：5
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