Synthesis and biological evaluation of coumarin derivatives as α-glucosidase inhibitors

In this study, two series of coumarin derivatives 5a∼i and 6a∼i were synthesized, and their inhibitory activity against α-glucosidase was determined. The results indicated that most of the synthesized derivatives exhibited prominent inhibitory activities against α-glucosidase. Among them, compounds...

Full description

Saved in:
Bibliographic Details
Published in:European journal of medicinal chemistry 2020-03, Vol.189, p.112013-112013, Article 112013
Main Authors: Xu, Xue-Tao, Deng, Xu-Yang, Chen, Jie, Liang, Qi-Ming, Zhang, Kun, Li, Dong-Li, Wu, Pan-Pan, Zheng, Xi, Zhou, Ren-Ping, Jiang, Zheng-Yun, Ma, Ai-Jun, Chen, Wen-Hua, Wang, Shao-Hua
Format: Article
Language:English
Subjects:
Cinnamic acid
Coumarin
Enzyme inhibition
Molecular docking
Synthesis
α-Glucosidase
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In this study, two series of coumarin derivatives 5a∼i and 6a∼i were synthesized, and their inhibitory activity against α-glucosidase was determined. The results indicated that most of the synthesized derivatives exhibited prominent inhibitory activities against α-glucosidase. Among them, compounds 5a and 5b showed the strongest inhibition with the IC50 values of 19.64 μM and 12.98 μM, respectively. Enzyme kinetic studies of compounds 5a and 5b proved that their inhibition was reversible and a mixed type. The KI and KIS values of compound 5a were calculated to be 27.39 μM and 13.02 μM, respectively, and the corresponding values for compound 5b being 27.02 μM and 13.65 μM, respectively. The docking studies showed that compound 5b could be inserted into the active pocket of α-glucosidase and form hydrogen bonds with LYS293 to enhance the binding affinity. [Display omitted] •Coumarin derivatives 5 (a ∼ i) and 6 (a ∼ i) were synthesized.•The synthetic compounds were screened for α-glucosidase inhibitory activity.•Kinetic studies determined the mechanism of synthetic compounds on α-glucosidase.•In silico studies were performed to confirm the binding interactions of synthetic compounds with the enzyme active site.
ISSN:0223-5234
1768-3254
DOI:10.1016/j.ejmech.2019.112013