INHIBITORY POTENTIAL OF CHEMICAL CONSTITUENTS FROM Paeonia suffruticosa AGAINST α-GLUCOSIDASE AND α-AMYLASE

被引:1
|
作者
Chen, Po-Chun [1 ,2 ]
Dlamini, Bongani Sicelo [3 ]
Chen, Chiy-Rong [4 ]
Shih, Wen-Ling [5 ]
Lee, Chien-Hsing [6 ,7 ,8 ]
Chang, Chi-, I [5 ]
机构
[1] Pingtung Christian Hosp, Dept Radiat Oncol, Pingtung 90054, Taiwan
[2] Natl Pingtung Univ Sci & Technol, Grad Inst Bioresources, Pingtung 91201, Taiwan
[3] Natl Pingtung Univ Sci & Technol, Dept Trop Agr & Int Cooperat, Pingtung 91201, Taiwan
[4] Natl Taitung Univ, Dept Life Sci, Taitung 95002, Taiwan
[5] Natl Pingtung Univ Sci & Technol, Dept Biol Sci & Technol, Pingtung 91201, Taiwan
[6] Kaohsiung Med Univ, Coll Med, Grad Inst Med, Dept Pharmacol, Kaohsiung 80708, Taiwan
[7] Kaohsiung Med Univ, Kaohsiung Med Univ Hosp, Dept Pharmacol, Sch Med, Kaohsiung 80708, Taiwan
[8] Kaohsiung Med Univ, Kaohsiung Med Univ Hosp, Coll Med, Sch Postbaccalaureate Med,Dept Med Res, Kaohsiung 80708, Taiwan
关键词
enzymatic activity; alpha-glucosidase inhibitor; Paeonia suffruticosa; spectroscopic analysis; MECHANISM;
D O I
10.1007/s11094-022-02715-x
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
Phytochemical study of the root bark of Paeonia suffruticosa plant led to the isolation and characterization of paeoniflorigenone (1), benzoylpaeoniflorin (2), betulinic acid (3), oleanolic acid (4), beta-sitosterol (5), and caffeic acid octadecyl ester (6). The enzymatic activities of compounds 1-6 were evaluated by in vitro inhibition assay of alpha-glucosidase and alpha-amylase. Compounds 1-6 with IC50 values ranging from 30 to 180 mu M inhibited alpha-glucosidase more efficiently than the standard compound acarbose (IC50 = 1463.0 +/- 29.5 mu M). Conversely, these compounds (with IC50 values ranging from 40 to 200 mu M) were less potent against alpha-amylase compared to acarbose (IC50 = 16.6 +/- 0.9 mu M). Kinetic analysis showed that compound 1 was a mixed-type inhibitor, compounds 3 and 4 were noncompetitive inhibitors, while compound 6 was an uncompetitive inhibitor of glucosidase.
引用
收藏
页码:821 / 826
页数:6
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