Structure related α-glucosidase inhibitory activity and molecular docking analyses of phenolic compounds from Paeonia suffruticosa

Abstract

In the continuous search for α-glucosidase inhibitors, eleven phenolic compounds (1-11) were isolated from the root bark of Paeonia suffruticosa. Their α-glucosidase inhibitory activity and inhibition mechanism were investigated using an in vitro inhibition assay and molecular docking studies. Compounds 2, 5, 6, and 8-11 (IC 50 between 290 and 431 µM) inhibited α-glucosidase more effectively than the reference compound acarbose (IC 50 =1463 ± 29.5 µM). Among them, compound 10 exhibited the highest α-glucosidase inhibitory effect with an IC 50 value of 290.4 ± 9.6 µM. Compounds 2, 5, 9 10 and 11 were found to be competitive inhibitors, while compounds 6 and 8 were noncompetitive inhibitors of α-glucosidase. Computational analyses showed that the main binding forces between the compounds and the main residues were hydrogen bonds. The results indicated that these compounds had considerable α-glucosidase inhibitory activity.

Screening for α-Glucosidase-Inhibiting Saponins from Pressurized Hot Water Extracts of Quinoa Husks

“…The crystal structure of isomaltose was downloaded from the Protein databank (PDB ID: 3A4A). A stable receptor was created with AutoDock by adding hydrogen atoms and removing water and ligands to modify the protein [30]. ChemBio 3D Ultra 19.0 was used to create the 3D structures of the compounds and standard acarbose, and the energy minimization was performed to obtain a reasonable conformation.…”