Urease is essential to Helicobacter pylori metabolism and plays role in stomach cancer, gastritis, peptic ulcer, hepatic coma, urinary tract infection, liver encephalopathy, and pyelonephritis. Therefore, inhibition of urease is an appealing approach to treat bacterial infections. The present work describes the synthesis of a series of ten new bioactive isatin-thiazole conjugates (5a-j). The target adducts were characterized using fourier transform infrared (FT-IR), ¹H- and ¹³C- nuclear magnetic resonance imaging (NMR) spectroscopy. The compounds were obtained using a multistep strategy that included nitration, alkylation, condensation and cyclization sequence. Subsequently, these compounds were screened for their urease inhibition potential. 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.

Urease is essential to Helicobacter pylori metabolism and plays role in stomach cancer, gastritis, peptic ulcer, hepatic coma, urinary tract infection, liver encephalopathy, and pyelonephritis. Therefore, inhibition of urease is an appealing approach to treat bacterial infections. The present work describes the synthesis of a series of ten new bioactive isatin-thiazole conjugates (5a-j). The target adducts were characterized using fourier transform infrared (FT-IR), ¹H- and ¹³C- nuclear magnetic resonance imaging (NMR) spectroscopy. The compounds were obtained using a multistep strategy that included nitration, alkylation, condensation and cyclization sequence. Subsequently, these compounds were screened for their urease inhibition potential. 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.

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.