Synthesis of benzimidazole derivatives as potent β-glucuronidase inhibitors

Synthesis of benzimidazole derivatives as potent β-glucuronidase inhibitors

Twenty five 4, 6-dichlorobenzimidazole derivatives (1-25) have been synthesized and evaluated against β-glucuronidase inhibitory activity. The compounds which actively inhibit β-glucuronidase activity have IC50 values ranging between 4.48 and 46.12 μM and showing better than standard d-saccharic aci...

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Published in:Bioorganic Chemistry
Main Author: Taha M.; Ismail N.H.; Imran S.; Selvaraj M.; Rashwan H.; Farhanah F.U.; Rahim F.; Kesavanarayanan K.S.; Ali M.
Format: Article
Language:English
Published: Academic Press Inc. 2015
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-84930958744&doi=10.1016%2fj.bioorg.2015.05.010&partnerID=40&md5=c5aa5ef1ca388142a22315a24df9e17f
id 2-s2.0-84930958744
spelling 2-s2.0-84930958744
Taha M.; Ismail N.H.; Imran S.; Selvaraj M.; Rashwan H.; Farhanah F.U.; Rahim F.; Kesavanarayanan K.S.; Ali M.
Synthesis of benzimidazole derivatives as potent β-glucuronidase inhibitors
2015
Bioorganic Chemistry
61

10.1016/j.bioorg.2015.05.010
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84930958744&doi=10.1016%2fj.bioorg.2015.05.010&partnerID=40&md5=c5aa5ef1ca388142a22315a24df9e17f
Twenty five 4, 6-dichlorobenzimidazole derivatives (1-25) have been synthesized and evaluated against β-glucuronidase inhibitory activity. The compounds which actively inhibit β-glucuronidase activity have IC50 values ranging between 4.48 and 46.12 μM and showing better than standard d-saccharic acid 1,4 lactone (IC50 = 48.4 ± 1.25 μM). Molecular docking provided potential clues to identify interactions between the active molecules and the enzyme which further led us to identify plausible binding mode of all the benzimidazole derivatives. This study confirmed that presence of hydrophilic moieties is crucial to inhibit the human β-glucuronidase. © 2015 Elsevier Inc. All rights reserved.
Academic Press Inc.
452068
English
Article
author Taha M.; Ismail N.H.; Imran S.; Selvaraj M.; Rashwan H.; Farhanah F.U.; Rahim F.; Kesavanarayanan K.S.; Ali M.
spellingShingle Taha M.; Ismail N.H.; Imran S.; Selvaraj M.; Rashwan H.; Farhanah F.U.; Rahim F.; Kesavanarayanan K.S.; Ali M.
Synthesis of benzimidazole derivatives as potent β-glucuronidase inhibitors
author_facet Taha M.; Ismail N.H.; Imran S.; Selvaraj M.; Rashwan H.; Farhanah F.U.; Rahim F.; Kesavanarayanan K.S.; Ali M.
author_sort Taha M.; Ismail N.H.; Imran S.; Selvaraj M.; Rashwan H.; Farhanah F.U.; Rahim F.; Kesavanarayanan K.S.; Ali M.
title Synthesis of benzimidazole derivatives as potent β-glucuronidase inhibitors
title_short Synthesis of benzimidazole derivatives as potent β-glucuronidase inhibitors
title_full Synthesis of benzimidazole derivatives as potent β-glucuronidase inhibitors
title_fullStr Synthesis of benzimidazole derivatives as potent β-glucuronidase inhibitors
title_full_unstemmed Synthesis of benzimidazole derivatives as potent β-glucuronidase inhibitors
title_sort Synthesis of benzimidazole derivatives as potent β-glucuronidase inhibitors
publishDate 2015
container_title Bioorganic Chemistry
container_volume 61
container_issue
doi_str_mv 10.1016/j.bioorg.2015.05.010
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-84930958744&doi=10.1016%2fj.bioorg.2015.05.010&partnerID=40&md5=c5aa5ef1ca388142a22315a24df9e17f
description Twenty five 4, 6-dichlorobenzimidazole derivatives (1-25) have been synthesized and evaluated against β-glucuronidase inhibitory activity. The compounds which actively inhibit β-glucuronidase activity have IC50 values ranging between 4.48 and 46.12 μM and showing better than standard d-saccharic acid 1,4 lactone (IC50 = 48.4 ± 1.25 μM). Molecular docking provided potential clues to identify interactions between the active molecules and the enzyme which further led us to identify plausible binding mode of all the benzimidazole derivatives. This study confirmed that presence of hydrophilic moieties is crucial to inhibit the human β-glucuronidase. © 2015 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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