Abstract
Modeled mode of binding of most active compound 9 (Magenta) into the active site of urease from Bacillus pasteurii. (A) Ribbon form. (B) Docked conformation showing interactions with Ni bi-center. (C) Surface form. [Display omitted]
•Acyl and Sulfonated coumarin derivatives are synthesized.•Compounds are evaluated for their urease inhibitory potential.•SAR is established on the basis of Molecular Modeling studies.•A comparison with previously synthesized biscoumarins is also provided.•New coumarin derivatives proved better inhibitors of urease as compared to previous biscoumarin derivatives.
Sixteen 4-hydroxycoumarin derivatives were synthesized, characterized through EI-MS and 1H NMR and screened for urease inhibitory potential. Three compounds exhibited better urease inhibition than the standard inhibitor thiourea (IC50=21±0.11μM) while other four compounds exhibited good to moderate inhibition with IC50 values between 29.45±1.1μM and 69.53±0.9μM. Structure activity relationship was established on the basis of molecular docking studies, which helped to predict the binding interactions of the most active compounds.