Inhibitory activity and mechanism of calycosin and calycosin-7-O-β-D-glucoside on α-glucosidase: Spectroscopic and molecular docking analyses

被引:21
作者
Han, Lingling [1 ]
Song, Jiaqi [1 ]
Yan, Chaoqun [1 ]
Wang, Chunqiang [1 ,3 ]
Wang, Liwei [1 ]
Li, Wen [1 ]
Du, Yan [1 ]
Li, Qingshan [1 ,2 ]
Liang, Taigang [1 ,2 ]
机构
[1] Shanxi Med Univ, Sch Pharmaceut Sci, 56 Xinjian Nan Rd, Taiyuan 030001, Shanxi, Peoples R China
[2] Shanxi Univ Tradit Chinese Med, 121 Univ St, Jinzhong 030619, Shanxi, Peoples R China
[3] Shanxi Med Univ, Dept Crit Care Med, Peoples Republ, Affiliated Hosp 1, 85 South Jiefang Rd, Taiyuan 030001, Shanxi, Peoples R China
关键词
Calycosin-7-O-?-D-glucoside; Calycosin; -Glucosidase; Inhibitory activity; Inhibitory mechanism; KINETICS; PHARMACOLOGY; ROOT;
D O I
10.1016/j.procbio.2022.04.035
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Inhibition of alpha-glucosidase activity plays a key role in reducing blood glucose level of type II diabetic patients. In study, the inhibitory activity and mechanism of Calycosin (CA) and calycosin-7-O-beta-D-glucoside (CAG), active components from Astragalus membranaceus, against alpha-glucosidase were studied by alpha-glucosidase activity tests, spectral analysis and docking simulation studies. The results suggested that the alpha-glucosidase inhibitory activity of CA (IC50 =39.45 mu M) and CAG (IC50 =174.04 mu M) were superior to acarbose (positive drug, IC50 =471.73 mu M). Fluorescence data indicated that CA and CAG quenched the fluorescence of alpha-glucosidase by spontaneous forming CA-alpha-glucosidase and CAG-alpha-glucosidase complexes. Besides, results obtained from CD and FT-IR analysis showed that the binding of CA or CAG to alpha-glucosidase caused conformational changes of alpha-glucosidase. Docking simulation results further suggested that, compared with CAG, CA had higher affinity for alpha-glucosidase because of its tightly bound to residues in active cavity of alpha-glucosidase. These findings demonstrated the alpha-glucosidase inhibitory activity and mechanism of CA and CAG, moreover, provided the basis for structural modification of AM flavonoids in the treatment of diabetes mellitus.
引用
收藏
页码:227 / 235
页数:9
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