Synthesis of 2-acylated and sulfonated 4-hydroxycoumarins: In vitro urease inhibition and molecular docking studies

Synthesis of 2-acylated and sulfonated 4-hydroxycoumarins: In vitro urease inhibition and molecular docking studies

Sixteen 4-hydroxycoumarin derivatives were synthesized, characterized through EI-MS and 1H NMR and screened for urease inhibitory potential. Three compounds exhibited better urease inhibition than the standard inhibitor thiourea (IC50 = 21 ± 0.11 μM) while other four compounds exhibited good to mode...

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Published in:Bioorganic Chemistry
Main Author: Rashid U.; Rahim F.; Taha M.; Arshad M.; Ullah H.; Mahmood T.; Ali M.
Format: Article
Language:English
Published: Academic Press Inc. 2016
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-84964603375&doi=10.1016%2fj.bioorg.2016.04.005&partnerID=40&md5=bb0716aef0a0dcb3380dd417b648b584
id 2-s2.0-84964603375
spelling 2-s2.0-84964603375
Rashid U.; Rahim F.; Taha M.; Arshad M.; Ullah H.; Mahmood T.; Ali M.
Synthesis of 2-acylated and sulfonated 4-hydroxycoumarins: In vitro urease inhibition and molecular docking studies
2016
Bioorganic Chemistry
66

10.1016/j.bioorg.2016.04.005
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84964603375&doi=10.1016%2fj.bioorg.2016.04.005&partnerID=40&md5=bb0716aef0a0dcb3380dd417b648b584
Sixteen 4-hydroxycoumarin derivatives were synthesized, characterized through EI-MS and 1H NMR and screened for urease inhibitory potential. Three compounds exhibited better urease inhibition than the standard inhibitor thiourea (IC50 = 21 ± 0.11 μM) while other four compounds exhibited good to moderate inhibition with IC50 values between 29.45 ± 1.1 μM and 69.53 ± 0.9 μM. Structure activity relationship was established on the basis of molecular docking studies, which helped to predict the binding interactions of the most active compounds. © 2016 Elsevier Inc. All rights reserved.
Academic Press Inc.
452068
English
Article
author Rashid U.; Rahim F.; Taha M.; Arshad M.; Ullah H.; Mahmood T.; Ali M.
spellingShingle Rashid U.; Rahim F.; Taha M.; Arshad M.; Ullah H.; Mahmood T.; Ali M.
Synthesis of 2-acylated and sulfonated 4-hydroxycoumarins: In vitro urease inhibition and molecular docking studies
author_facet Rashid U.; Rahim F.; Taha M.; Arshad M.; Ullah H.; Mahmood T.; Ali M.
author_sort Rashid U.; Rahim F.; Taha M.; Arshad M.; Ullah H.; Mahmood T.; Ali M.
title Synthesis of 2-acylated and sulfonated 4-hydroxycoumarins: In vitro urease inhibition and molecular docking studies
title_short Synthesis of 2-acylated and sulfonated 4-hydroxycoumarins: In vitro urease inhibition and molecular docking studies
title_full Synthesis of 2-acylated and sulfonated 4-hydroxycoumarins: In vitro urease inhibition and molecular docking studies
title_fullStr Synthesis of 2-acylated and sulfonated 4-hydroxycoumarins: In vitro urease inhibition and molecular docking studies
title_full_unstemmed Synthesis of 2-acylated and sulfonated 4-hydroxycoumarins: In vitro urease inhibition and molecular docking studies
title_sort Synthesis of 2-acylated and sulfonated 4-hydroxycoumarins: In vitro urease inhibition and molecular docking studies
publishDate 2016
container_title Bioorganic Chemistry
container_volume 66
container_issue
doi_str_mv 10.1016/j.bioorg.2016.04.005
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-84964603375&doi=10.1016%2fj.bioorg.2016.04.005&partnerID=40&md5=bb0716aef0a0dcb3380dd417b648b584
description Sixteen 4-hydroxycoumarin derivatives were synthesized, characterized through EI-MS and 1H NMR and screened for urease inhibitory potential. Three compounds exhibited better urease inhibition than the standard inhibitor thiourea (IC50 = 21 ± 0.11 μM) while other four compounds exhibited good to moderate inhibition with IC50 values between 29.45 ± 1.1 μM and 69.53 ± 0.9 μM. Structure activity relationship was established on the basis of molecular docking studies, which helped to predict the binding interactions of the most active compounds. © 2016 Elsevier Inc. All rights reserved.
publisher Academic Press Inc.
issn 452068
language English
format Article
accesstype
record_format scopus
collection Scopus
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