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Morning glory resin glycosides as α-glucosidase inhibitors: In vitro and in silico analysis

Rosas-Ramírez, Daniel, Escandón-Rivera, Sonia, Pereda-Miranda, Rogelio
Phytochemistry 2018 v.148 pp. 39-47
Convolvulaceae, Saccharomyces cerevisiae, acarbose, active ingredients, active sites, alpha-glucosidase, amino acids, disease control, enzyme inhibition, enzyme inhibitors, glycemic effect, glycosides, humans, hydrogen bonding, molecular models, phytotherapy, yeasts
Twenty-seven individual resin glycosides from the morning glory family (Convolvulaceae) were evaluated for their α-glucosidase inhibitory potential. Four of these compounds displayed an inhibitory activity comparable to acarbose, which was used as a positive control. Molecular modeling studies performed by docking analysis were accomplished to predict that the active compounds and acarbose bind to the α-1,4-glucosidase enzyme catalytic site of MAL12 from the yeast Saccharomyces cerevisiae through stable hydrogen bonds primarily with the amino acid residues HIS279 and GLN322. Docking studies with the human maltase-glucoamylase (MGAM) also identified binding modes for resin glycosides inside the catalytic site in the proximity of TYR1251. These results postulate that resin glycosides may be a source of phytotherapeutic agents with antihyperglycemic properties for the prophylaxis and treatment of non-insulin-dependent type 2 diabetes mellitus.