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

页码：799 / 803

页数：5

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