Urease inhibitory activities of β-boswellic acid derivatives
| Autor: | Farzaneh Nabati, Massoud Amanlou, Zinat Bahrampour Omrany, Sahand Golestanian, Shamsali Rezazadeh, Reza Hajiaghaee, Behnam Yousefi, Roya Bazl, Sanaz Golbabaei |
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| Rok vydání: | 2013 |
| Předmět: |
Boswellia carterii
Urease biology business.industry Pharmacology toxicology Urease inhibitor Boswellic acid Building and Construction Pharmacology Inhibitory postsynaptic potential Docking chemistry.chemical_compound chemistry Docking (molecular) biology.protein Medicine business Research Article Autodock |
| Zdroj: | DARU Journal of Pharmaceutical Sciences |
| ISSN: | 2008-2231 |
| DOI: | 10.1186/2008-2231-21-2 |
| Popis: | Background and the purpose of the study Boswellia carterii have been used in traditional medicine for many years for management different gastrointestinal disorders. In this study, we wish to report urease inhibitory activity of four isolated compound of boswellic acid derivative. Methods 4 pentacyclic triterpenoid acids were isolated from Boswellia carterii and identified by NMR and Mass spectroscopic analysis (compounds 1, 3-O-acetyl-9,11-dehydro-β-boswellic acid; 2, 3-O-acetyl-11-hydroxy-β-boswellic acid; 3. 3-O- acetyl-11-keto-β-boswellic acid and 4, 11-keto-β-boswellic acid. Their inhibitory activity on Jack bean urease were evaluated. Docking and pharmacophore analysis using AutoDock 4.2 and Ligandscout 3.03 programs were also performed to explain possible mechanism of interaction between isolated compounds and urease enzyme. Results It was found that compound 1 has the strongest inhibitory activity against Jack bean urease (IC50 = 6.27 ± 0.03 μM), compared with thiourea as a standard inhibitor (IC50 = 21.1 ± 0.3 μM). Conclusion The inhibition potency is probably due to the formation of appropriate hydrogen bonds and hydrophobic interactions between the investigated compounds and urease enzyme active site and confirms its traditional usage. |
| Databáze: | OpenAIRE |
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