Wedtrilosides A and B, two new diterpenoid glycosides from the leaves of Wedelia trilobata (L.) Hitchc. with α-amylase and α-glucosidase inhibitory activities

被引:18
|
作者
Nguyen Thi Luyen [1 ,2 ,3 ]
Pham Thanh Binh [1 ]
Pham Thi Tham [4 ]
Ta Manh Hung [5 ]
Nguyen Hai Dang [1 ,3 ]
Nguyen Tien Dat [2 ,3 ]
Nguyen Phuong Thao [1 ]
机构
[1] VAST, Inst Marine Biochem IMBC, 18 Hoang Quoc Viet, Hanoi, Vietnam
[2] VAST, Ctr Res & Technol Transfer, 18 Hoang Quoc Viet, Hanoi, Vietnam
[3] VAST, Grad Univ Sci & Technol, 18 Hoang Quoc Viet, Hanoi, Vietnam
[4] Hanoi Univ Ind, Fac Chem Technol, 298 Cau Dien, Hanoi, Vietnam
[5] NIDQC, 48 Hai Ba Trung, Hanoi, Vietnam
关键词
Wedelia trilobata; Asteraceae; Wedtrilosides A-B; alpha-Amylase activity; alpha-Glucosidase activity; ACID;
D O I
10.1016/j.bioorg.2019.01.010
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
In the ongoing research to find new diabetes constituents from the genus Wedelia, the chemical constituent of Wedelia trilobata leaves, a Vietnamese medicinal plant species used to treat type 2 diabetes mellitus, was selected for detailed investigation. From a methanolic extract, two new ent-kaurane diterpenoids, wedtrilosides A and B (1 and 2), along with five known metabolites (3-7), were isolated from W. trilobata. The chemical structures of (1-7) were assigned via spectroscopic techniques (IR, 1D, 2D NMR and HR-QTOF-MS data) and chemical methods. The isolates were evaluated for alpha-amylase and alpha-glucosidase inhibitory activities compared to the clinical drug acarbose. Among them, compounds 4, 6, and 7 showed the most potent against alpha-glucosidase enzyme with IC50 values of 27.54 +/- 1.12, 173.78 +/- 2.37, and 190.40 +/- 2.01 mu g/mL. While moderate inhibitory effect against alpha-amylase was observed with compounds 6 and 7 (with IC50 = 181.97 +/- 2.62 and 52.08 +/- 0.56 mu g/mL, respectively). The results suggested that the antidiabetic properties from the leaves of W. trilobata are not simply a result of each isolated compound, but are due to other factors such as the accessibility of polyphenolic groups to alpha-amylase and alpha-glucosidase activities.
引用
收藏
页码:319 / 324
页数:6
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