Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton

In our effort directed toward the discovery of new anti-diabetic agent for the treatment of diabetes, a library of biscoumarin derivative 1-18 was synthesized and evaluated for α-glucosidase inhibitory potential. All eighteen (18) compounds displayed assorted α-glucosidase activity with IC50 values...

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Published in:European Journal of Medicinal Chemistry
Main Author: Khan K.M.; Rahim F.; Wadood A.; Kosar N.; Taha M.; Lalani S.; Khan A.; Fakhri M.I.; Junaid M.; Rehman W.; Khan M.; Perveen S.; Sajid M.; Choudhary M.I.
Format: Article
Language:English
Published: Elsevier Masson SAS 2014
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-84901047505&doi=10.1016%2fj.ejmech.2014.05.010&partnerID=40&md5=f812216d7ea4978dcf86e9b7983709e8
id 2-s2.0-84901047505
spelling 2-s2.0-84901047505
Khan K.M.; Rahim F.; Wadood A.; Kosar N.; Taha M.; Lalani S.; Khan A.; Fakhri M.I.; Junaid M.; Rehman W.; Khan M.; Perveen S.; Sajid M.; Choudhary M.I.
Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton
2014
European Journal of Medicinal Chemistry
81

10.1016/j.ejmech.2014.05.010
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84901047505&doi=10.1016%2fj.ejmech.2014.05.010&partnerID=40&md5=f812216d7ea4978dcf86e9b7983709e8
In our effort directed toward the discovery of new anti-diabetic agent for the treatment of diabetes, a library of biscoumarin derivative 1-18 was synthesized and evaluated for α-glucosidase inhibitory potential. All eighteen (18) compounds displayed assorted α-glucosidase activity with IC50 values 16.5-385.9 μM, if compared with the standard acarbose (IC50 = 906 ± 6.387 μM). In addition, molecular docking studies were carried out to explore the binding interactions of biscoumarin derivatives with the enzyme. This study has identified a new class of potent α-glucosidase inhibitors. © 2014 Elsevier Masson SAS. All rights reserved.
Elsevier Masson SAS
2235234
English
Article

author Khan K.M.; Rahim F.; Wadood A.; Kosar N.; Taha M.; Lalani S.; Khan A.; Fakhri M.I.; Junaid M.; Rehman W.; Khan M.; Perveen S.; Sajid M.; Choudhary M.I.
spellingShingle Khan K.M.; Rahim F.; Wadood A.; Kosar N.; Taha M.; Lalani S.; Khan A.; Fakhri M.I.; Junaid M.; Rehman W.; Khan M.; Perveen S.; Sajid M.; Choudhary M.I.
Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton
author_facet Khan K.M.; Rahim F.; Wadood A.; Kosar N.; Taha M.; Lalani S.; Khan A.; Fakhri M.I.; Junaid M.; Rehman W.; Khan M.; Perveen S.; Sajid M.; Choudhary M.I.
author_sort Khan K.M.; Rahim F.; Wadood A.; Kosar N.; Taha M.; Lalani S.; Khan A.; Fakhri M.I.; Junaid M.; Rehman W.; Khan M.; Perveen S.; Sajid M.; Choudhary M.I.
title Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton
title_short Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton
title_full Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton
title_fullStr Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton
title_full_unstemmed Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton
title_sort Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton
publishDate 2014
container_title European Journal of Medicinal Chemistry
container_volume 81
container_issue
doi_str_mv 10.1016/j.ejmech.2014.05.010
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-84901047505&doi=10.1016%2fj.ejmech.2014.05.010&partnerID=40&md5=f812216d7ea4978dcf86e9b7983709e8
description In our effort directed toward the discovery of new anti-diabetic agent for the treatment of diabetes, a library of biscoumarin derivative 1-18 was synthesized and evaluated for α-glucosidase inhibitory potential. All eighteen (18) compounds displayed assorted α-glucosidase activity with IC50 values 16.5-385.9 μM, if compared with the standard acarbose (IC50 = 906 ± 6.387 μM). In addition, molecular docking studies were carried out to explore the binding interactions of biscoumarin derivatives with the enzyme. This study has identified a new class of potent α-glucosidase inhibitors. © 2014 Elsevier Masson SAS. All rights reserved.
publisher Elsevier Masson SAS
issn 2235234
language English
format Article
accesstype
record_format scopus
collection Scopus
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