Structural basis of binding and justification for the urease inhibitory activity of acetamide hybrids of N-substituted 1,3,4-oxadiazoles and piperidines

In present, we have performed the Michaelis–Menten kinetics studies of urease inhibitors (6a–o), having basic skeleton of acetamide hybrids of N-substituted 1,3,4-oxadiazoles and piperidines. From the Lineweaver-Burk plot, Dixon plot and their secondary replots, it has been confirmed that all the co...

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Bibliographic Details
Published in:Journal of molecular structure 2021-01, Vol.1223, p.129141, Article 129141
Main Authors: Khan, Farman Ali, Rehman, Aziz Ur, Abbasi, Muhammad Athar, Afridi, Sahib Gul, Khan, Asifullah, Lodhi, Muhammad Arif, Khan, Ajmal
Format: Article
Language:English
Subjects:
Acetamide hybrids
Cytotoxicity
Enzyme kinetics
Oxadiazole
Phytotoxicity
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Summary:In present, we have performed the Michaelis–Menten kinetics studies of urease inhibitors (6a–o), having basic skeleton of acetamide hybrids of N-substituted 1,3,4-oxadiazoles and piperidines. From the Lineweaver-Burk plot, Dixon plot and their secondary replots, it has been confirmed that all the compounds have inhibited the enzyme competitively with Ki values of in range from 3.11 ± 0.2 to 5.20 ± 0.7 μM. Compound 6a was found to have lowest Ki among the series, while compounds 6d, 6e, 6gand 6i were found subsequently the excellent Ki values after 6a. Molecular docking has supported their types of inhibitions and structure activity-relationship. Most frequently, the nitro group oxygen atoms were found in contact with nickel ions of the active site. Moreover, all the compounds were subjected to toxicity tests and were found nontoxic against human neutrophils and plants, respectively.
ISSN:0022-2860
1872-8014
DOI:10.1016/j.molstruc.2020.129141