Rapid screening of α-glucosidase inhibitors in Hypericum perforatum L. by bio-affinity chromatography coupled with UPLC/MS

In this study, the extract of Hypericum perforatum L. (HPE) has been confirmed to have α-glucosidase inhibitory activity in vitro and in vivo. Seven active compounds including rutin, hyperoside, isoquercitrin, avicularin, quercitrin, quercetin, and biapigenin were screened based on a bio-affinity chromatography column with α-glucosidase enzyme-conjugated solid phase and UPLC/MS, which exhibited excellent α-glycosidase inhibitory effects by the determined IC50 values. The mechanism of α-glycosidase inhibitory activity of biapigenin was studied for the first time. The results showed that biapigenin was a high potential reversible and mixed enzyme inhibitor. Analysis by molecular docking further revealed that hydrophobic interactions were generated by interactions between biapigenin and amino acid residues LYS156, PHE303, PHE314 and LEU313. In addition, hydrogen bonding occurred between biapigenin and α-glucosidase amino acid residues ASP307, SER241 and LYS156. This research identified that biapigenin could be a novel α-glucosidase inhibitor and further applied to the development of potential anti-diabetic drugs. Furthermore, our studies established a rapid in vitro screening method for AGIs from plants.PMID:36264709 | DOI:10.1002/bmc.5536
Source: Biomedical Chromatography : BMC - Category: Biomedical Science Authors: Source Type: research