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...
Published in: | European Journal of Medicinal Chemistry |
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Elsevier Masson SAS
2014
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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 |
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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 |
_version_ |
1809678487944953856 |