Wedtrilosides A and B, two new diterpenoid glycosides from the leaves of Wedelia trilobata (L.) Hitchc. with α-amylase and α-glucosidase inhibitory activities
| Autor: | Pham Thi Tham, Nguyen Hai Dang, Nguyen Tien Dat, Nguyen Phuong Thao, Pham Thanh Binh, Ta Manh Hung, Nguyen Thi Luyen |
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| Rok vydání: | 2019 |
| Předmět: |
01 natural sciences
Biochemistry Wedelia Drug Discovery medicine Hypoglycemic Agents Glycoside Hydrolase Inhibitors Glycosides Amylase Molecular Biology Acarbose chemistry.chemical_classification Plants Medicinal biology Traditional medicine 010405 organic chemistry Organic Chemistry Glycoside Asteraceae biology.organism_classification Terpenoid 0104 chemical sciences Plant Leaves 010404 medicinal & biomolecular chemistry chemistry Wedelia trilobata Polyphenol biology.protein Diterpenes alpha-Amylases medicine.drug |
| Zdroj: | Bioorganic Chemistry. 85:319-324 |
| ISSN: | 0045-2068 |
| Popis: | 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 α-amylase and α-glucosidase inhibitory activities compared to the clinical drug acarbose. Among them, compounds 4, 6, and 7 showed the most potent against α-glucosidase enzyme with IC50 values of 27.54 ± 1.12, 173.78 ± 2.37, and 190.40 ± 2.01 μg/mL. While moderate inhibitory effect against α-amylase was observed with compounds 6 and 7 (with IC50 = 181.97 ± 2.62 and 52.08 ± 0.56 μg/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 α-amylase and α-glucosidase activities. |
| Databáze: | OpenAIRE |
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