Abstract
In this study, the interaction between Luteolin and urease was made at 300 K in aqueous buffer solutions using isothermal titration calorimetry. The extended solvation model was used to calculate the solvation parameters. Moreover, to determine the interaction of Luteolin with Jack Bean Urease (JBU), a molecular docking process was performed. The purpose of this investigation was to measure the inhibitory effects of Luteolin on the activity and structure of urease. Molecular docking analysis confirmed the extended solvation model.
Highlights
In this study, the interaction between Luteolin and urease was made at 300 K in aqueous buffer solutions using isothermal titration calorimetry
To determine the interaction of Luteolin with Jack Bean Urease (JBU), a molecular docking process was performed. The purpose of this investigation was to measure the inhibitory effects of Luteolin on the activity and structure of urease
The question of finding effective and useful inhibitors of urease enzyme has been in the interest of researchers for many years
Summary
The question of finding effective and useful inhibitors of urease enzyme has been in the interest of researchers for many years. Received: 16 July 2020 Accepted: 26 September 2020 Published: 12 October 2020 Study of jack bean urease interaction with luteolin by the extended solvation model and docking simulation
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