Academic Journal
Synthesis and Evaluation of Isatin Analogs as Potential Urease and Tyrosinase Inhibitors: An Approach of Molecular Docking.
| Title: | Synthesis and Evaluation of Isatin Analogs as Potential Urease and Tyrosinase Inhibitors: An Approach of Molecular Docking. |
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| Authors: | Ma G; School of Chemistry & Materials Engineering, Xinxiang University, Xinxiang, Henan, China., Li Y; School of Pharmacy, Xinxiang University, Xinxiang, Henan, China., Xu S; School of Pharmacy, Xinxiang University, Xinxiang, Henan, China., Javid MT; Department of Chemistry, University of Layyah, Layyah, Punjab, Pakistan., Ahmed N; Department of Chemistry, PMAS-Aid Agriculture University, Rawalpindi, Pakistan., Farooq U; Miami College of Henan University, Kaifeng, Henan, China. |
| Source: | Chemistry & biodiversity [Chem Biodivers] 2026 May; Vol. 23 (5), pp. e71285. |
| Publication Type: | Journal Article |
| Language: | English |
| Journal Info: | Publisher: Verlag Helvetica Chimica Acta Country of Publication: Switzerland NLM ID: 101197449 Publication Model: Print Cited Medium: Internet ISSN: 1612-1880 (Electronic) Linking ISSN: 16121872 NLM ISO Abbreviation: Chem Biodivers Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Zürich, Switzerland : Hoboken, NJ : Verlag Helvetica Chimica Acta ; Distributed in the USA by Wiley, c2004- |
| MeSH Terms: | Urease*/antagonists & inhibitors , Urease*/metabolism , Isatin*/chemical synthesis , Isatin*/chemistry , Isatin*/pharmacology , Isatin*/analogs & derivatives , Monophenol Monooxygenase*/antagonists & inhibitors , Monophenol Monooxygenase*/metabolism , Enzyme Inhibitors*/chemical synthesis , Enzyme Inhibitors*/chemistry , Enzyme Inhibitors*/pharmacology , Molecular Docking Simulation*, Schiff Bases/chemistry ; Schiff Bases/chemical synthesis ; Schiff Bases/pharmacology ; Structure-Activity Relationship ; Molecular Structure ; Dose-Response Relationship, Drug |
| Abstract: | A series of isatin-based Schiff base derivatives (1-12) was synthesized via a two-step reaction and characterized using spectroscopic techniques such as 1H-NMR and mass spectrometry. The urease and tyrosinase inhibitory activities of the synthesized compounds were evaluated using thiourea (IC50 = 21.25 ± 0.15 µM) and kojic acid (IC50 = 121 ± 0.5 µM) as standard inhibitors. Among the synthesized analogs, only three compounds-1 (IC50 = 38.9 ± 0.06 µM), 3 (IC50 = 56.7 ± 0.02 µM), and 10 (IC50 = 71 ± 0.09 µM) showed moderate urease inhibition, while the remaining compounds were inactive. All compounds were inactive against tyrosinase inhibition. The structure-activity relationship (SAR) of the active analogs was established based on the nature, position, and number of substituents on the phenyl ring of the basic nucleus of the compounds. Molecular docking studies were performed to confirm the binding interactions of the most potent analogs with the active site of urease. The docking results revealed that compound 1 formed six strong intermolecular interactions with the binding site residues of urease, exhibiting the lowest docking score of -4.8944. The findings suggest that the synthesized isatin-based Schiff base derivatives, particularly compounds 1, 3, and 10, could serve as potential lead compounds for developing novel urease inhibitors. (© 2026 Wiley‐VHCA AG.) |
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| Grant Information: | 232102231034 Henan Provincial Key R&D; 23A150051 Henan Provincial Key scientific research project program |
| Contributed Indexing: | Keywords: SAR relationship; derivatives; isatin‐based Schiff bases; molecular docking; synthesis; urease and tyrosinase inhibition |
| Substance Nomenclature: | EC 3.5.1.5 (Urease) 82X95S7M06 (Isatin) EC 1.14.18.1 (Monophenol Monooxygenase) 0 (Enzyme Inhibitors) 0 (Schiff Bases) |
| Entry Date(s): | Date Created: 20260504 Date Completed: 20260716 Latest Revision: 20260726 |
| Update Code: | 20260726 |
| PubMed Central ID: | PMC13376694 |
| DOI: | 10.1002/cbdv.71285 |
| PMID: | 42081650 |
| Database: | MEDLINE |
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