Discovery of isatin-thiazole conjugates as potent urease inhibitors; synthesis, biochemical screening and computational studies

All the compounds showed better inhibitory potential than the positive control, thiourea with IC₅₀ ranging from 0.44 to 8.70 µM. However, compound 5j exhibited an excellent non-competitive urease inhibitory effect with an IC₅₀ value of 0.44 ± 0.23 µM. Apart from in vitro investigation, the molecular docking revealed a strong affinity of 5j within the active site of urease exhibiting a binding energy of -7.9 kcal/mol. Succinctly, the lead inhibitor 5j exhibited noteworthy IC₅₀ and effective binding free energy which emphasizes its strong binding potential. .