Understanding of the conformational flexibility and electrostatic properties of coumarin derivatives in the active site of S. cerevisiae α-glucosidase

Qi, Yanjiao; Lu, Huanjun; Jin, Neng-Zhi; Zhang, J. Y.; Dong, Jiajun

doi:10.1007/s00044-017-2086-4

Cited by 1 publication

(2 citation statements)

References 56 publications

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“…The hydrophobic interactions were formed by biapigenin with amino acid residues LYS156, PHE303, PHE314, and LEU313, and hydrogen bonds were formed between biapigenin and amino acid residues ASP307, SER241, and LYS156 (Figure 8). The results were consistent with those of the previous study on polyhydroxy compounds, and hydrogen bond interaction played a very important role in all binding modes (Leong et al, 2018; Qi et al, 2017). In addition, π–π bonds at Tyr158 were also formed, which could introduce larger binding ability and stronger binding force.…”

Section: Resultssupporting

confidence: 93%

“…formed between biapigenin and amino acid residues ASP307, SER241, and LYS156 (Figure 8). The results were consistent with those of the previous study on polyhydroxy compounds, and hydrogen bond interaction played a very important role in all binding modes (Leong et al, 2018;Qi et al, 2017). In addition, π-π bonds at Tyr158…”

Section: Inhibitory Mechanism Of Biapigenin On α-Glucosidase Activitysupporting

confidence: 92%

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

Dong

Yue

et al. 2022

Biomedical Chromatography

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α‐glucosidase inhibitors (AGIs) are widely used for the treatment of type 2 diabetes, but their side effects have made it to develop novel and alternative AGIs immediately. 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, 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 AGI 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.

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Section: Resultssupporting

confidence: 93%

Section: Inhibitory Mechanism Of Biapigenin On α-Glucosidase Activitysupporting

confidence: 92%

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

Dong

Yue

et al. 2022

Biomedical Chromatography

View full text Add to dashboard Cite

show abstract

Understanding of the conformational flexibility and electrostatic properties of coumarin derivatives in the active site of S. cerevisiae α-glucosidase

Cited by 1 publication

References 56 publications

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

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

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