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

被引：38

作者：

Rosas-Ramirez, Daniel ^{[1
]}

Escandon-Rivera, Sonia ^{[2
]}

Pereda-Miranda, Rogelio ^{[3
]}

机构：

[1] Univ Nacl Autonoma Mexico, Dept Quim Biomacromol, Inst Quim, Mexico City, DF, Mexico

[2] Univ Nacl Autonoma Mexico, Dept Biol Celular, Fac Ciencias, Mexico City, DF, Mexico

[3] Univ Nacl Autonoma Mexico, Dept Farm, Fac Quim, Ciudad Univ, Mexico City 04510, DF, Mexico

来源：

PHYTOCHEMISTRY | 2018年 / 148卷

关键词：

Resin glycoside; alpha-Glucosidase inhibition; Molecular docking; Glycolipid; ANTIBIOTIC-ACTIVITY; IPOMOEA; MODULATORS;

D O I：

10.1016/j.phytochem.2018.01.012

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：

Twenty-seven individual resin glycosides from the morning glory family (Convolvulaceae) were evaluated for their alpha-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 alpha-1,4-glucosidase enzyme catalytic site of MAL12 from the yeast Saccharomyces cerevisiae through stable hydrogen bonds primarily with the amino acid residues H1S279 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. (C) 2018 Elsevier Ltd. All rights reserved.

引用

页码：39 / 47

页数：9

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