A new feruloylfriedelinol from the stems of Bridelia stipularis and its α-glucosidase inhibition.

Autor: Limtragool OA; Multidisciplinary Research Unit of Pure and Applied Chemistry, Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Mahasarakham University, Maha Sarakham, Thailand., Pitchuanchom S; Multidisciplinary Research Unit of Pure and Applied Chemistry, Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Mahasarakham University, Maha Sarakham, Thailand., Saensouk S; Diversity of Family Zingiberaceae and Vascular Plant for Its Applications Research Unit, Walai Rukhavej Botanical Research Institute, Mahasarakham University, Maha Sarakham, Thailand., Poopasit K; Natural Products Research Unit, Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Khon Kaen University, Khon Kaen, Thailand., Kanokmedhakul K; Natural Products Research Unit, Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Khon Kaen University, Khon Kaen, Thailand., Kanokmedhakul S; Natural Products Research Unit, Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Khon Kaen University, Khon Kaen, Thailand.
Jazyk: angličtina
Zdroj: Natural product research [Nat Prod Res] 2024 Sep; Vol. 38 (18), pp. 3269-3274. Date of Electronic Publication: 2023 Jun 07.
DOI: 10.1080/14786419.2023.2222218
Abstrakt: Phytochemical investigation of the stems of Bridelia stipularis led to the isolation of a new triterpene, 3 β - O - trans -feruloylfriedelinol ( 1 ), together with five known compounds, friedelin ( 2 ), 3 β -friedelinol ( 3 ), lupeol ( 4 ), stigmasterol ( 5 ), and 4-(1,5-dimethyl-3-oxo-4-hexenyl)benzoic acid ( 6 ). Their structures were identified by intensive spectroscopic analysis including 1D and 2D nuclear magnetic resonance, infrared, and mass spectrometry. Compound 1 showed significant α-glucosidase inhibitory activity (IC 50 = 337.49 ± 0.59 µM) close to the standard, acarbose. Furthermore, the structure activity relationship of 1 was analyzed by molecular docking studies. In addition, the molecular docking results showed that the interaction between 1 and the active site occurred through hydrophobic forces and hydrogen bonds.
Databáze: MEDLINE