Alpha-Glucosidase inhibitory activity and molecular docking analysis of a new biflavan isolated from Impatiens
Duc Long Le1, Ba Thi Cham1, Thi Yen Tran1
1Institute of Chemistry, Vietnam Academy of Science and Technology (VAST), Hanoi, Viet Nam.
Abstract:
For the first time, Impatiens macrantha was investigated for chemical constituents to produce a new biflavan, namely macranthabiflavan A (1), and nine known compounds, 5-O-caffeoylquinic acid (2), 4,5-dicaffeoylquinic acid (3), spinasterol (4), spinasterone (5), β-amyrin acetate (6), apigenin (7), quercetin-3-O-β-D-glucopyranoside (8), 4-hydroxy-3-methoxy benzoic acid (9), and uridine (10). Their structures were elucidated by extensive spectroscopic analyses (1D- and 2D-NMR, HR ESI MS) and comparison with reported data. Using p-nitrophenyl-α-D-glucopyranoside as the substrate, compound 1 exhibited potent α-glucosidase inhibitory activity with an IC50 value of 13.08 ± 0.16 μg/mL, much more stronger than that of the positive control acarbose (IC50 197.5 ± 6.25 µg/mL). Molecular docking studies further revealed that compound 1 effectively occupies the catalytic pocket of maltase-glucoamylase (MGAM), indicating a mechanism of direct active-site inhibition. Notably, new compound 1 showed a higher binding affinity (-7.299 kcal/mol) than acarbose (-6.47 kcal/mol), suggesting more favourable interactions with key catalytic residues.
More Related Videos
13:18Network Pharmacology Prediction and Experimental Validation of Trichosanthes-Fritillaria thunbergii Action Mechanism Against Lung Adenocarcinoma
Published on: March 3, 2023
13:35Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
Published on: May 23, 2025
Related Concept Videos
Oral Hypoglycemic Agents: α-Glucosidase Inhibitors
Acarbose and miglitol are...
Antifungal Agents
Dipeptidyl Peptidase 4 Inhibitors
Enzyme Inhibition
