4.6 Article

An overview: metal-based inhibitors of urease

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TAYLOR & FRANCIS LTD
DOI: 10.1080/14756366.2022.2150182

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Urease; metal-based urease inhibitor; structure-activity relationship; molecular docking

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This review summarizes the metal-based inhibitors of urease, including the inhibition, structure-activity relationship, and molecular docking. Copper metal complexes exhibit strong urease inhibition and offer potential guidance for the development of novel inhibitors.
Urease is a kind of nickel-dependent metalloenzyme, which exists in the biological world widely, and can catalyse the hydrolysis of urea into ammonia and carbon dioxide to provide a nitrogen source for organisms. Urease has important uses in agriculture and medicine because it can catalyse the production of ammonia. Therefore, in this review, metal-based inhibitors of urease will be summarised according to different transition metal ions. Including the urease inhibition, structure-activity relationship, and molecular docking. Importantly, among these reviewed effective urease inhibitors, most of copper metal complexes exhibited stronger urease inhibition with IC50 values ranging from 0.46 mu M to 41.1 mu M. Significantly, the collected comprehensive information looks forward to providing rational guidance and effective strategies for the development of novel, potent, and safe metal-based urease inhibitors, which are better for practical applications in the future.

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