An expedient synthesis of N‐(1‐(5‐mercapto‐4‐((substituted benzylidene)amino)‐4H‐1, 2, 4‐triazol‐3‐yl)‐2‐phenylethyl)benzamides as jack bean urease inhibitors and free radical scavengers: Kinetic mechanism and molecular docking studies. (19th June 2017) - Saeed, Aamer
Abstract : In this study, some new azomethine‐triazole hybrids5a–5l derived from N ‐benzoyl‐L‐phenylalanine were synthesized and characterized. The synthesized compounds showed first‐rate, urease inhibition, and compounds5c and5e were found to be most effective inhibitors with 0.0137 ± 0.00082 μm and 0.0183 ± 0.00068 μm, respectively (thiourea 15.151 ± 1.27 μm ). The kinetic mechanism of urease inhibition revealed the compounds5c and5e to be non‐competitive inhibitors, whereas compounds5d and5j were found to be of mixed‐type inhibitors. Docking studies also indicated better interaction patterns with urease enzyme. The results of enzyme inhibition, kinetic mechanism and molecular docking suggest that these compounds can serve as lead compounds in the design of more effective urease inhibitors. Abstract : Synthesis of N ‐(1‐(5‐mercapto‐4‐((substituted benzylidene) amino)‐4 H ‐1, 2, 4‐triazol‐3‐yl)‐2‐phenylethyl) benzamides as jack bean urease and free radical scavenger inhibitors. Kinetic mechanism revealed that most potent derivative5j inhibits enzyme by non‐competitive mechanism. The binding affinity of the molecules was evaluated using molecular docking studies. Based on the results of enzyme inhibition activities and molecular docking, it was inferred that these molecules can serve as template for the drug designing and discovery. Further structural modifications to most potent derivatives can lead to the designing of efficient enzyme inhibitors.