title: Synthesis, biological assay in vitro and molecular docking studies of new Schiff base derivatives as potential urease inhibitors.
abstract: A series of new and novel Schiff base derivatives were synthesized and investigated as potential new inhibitors of Jack bean urease. The most potent compounds were 3f with (K(i) = 0.09 μM) and 3k (K(i) = 0.122 μM). A pure competitive mechanism of inhibition was observed. Molecular docking studies were also performed to illustrate the binding mode of the compounds. Docking studies were performed on both enzymes from Jack bean urease and H. pylori urease. It was observed that both share the same binding mode. The binding sites of the two urease structures also aligned very well indicating the similarity in binding sites of the enzymes.
authors: Department of Pharmaceutical Sciences, COMSATS Institute of Information Technology, Abbottabad, Postal Code 22060, Pakistan.
authors: Muhammad Adil S
authors: MA
authors: Aslam
authors: Shams-ul
authors: SU
authors: Mahmood
authors: Mohammad
authors: M
authors: Shahid
authors: Aamer
authors: A
authors: Saeed
authors: Jamshed
authors: J
authors: Iqbal
mesh_terms: D032449:Canavalia / Q000201:enzymology; D060326:Chemistry Techniques, Synthetic; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D020128:Inhibitory Concentration 50; D007700:Kinetics; D008958:Models, Molecular; D011487:Protein Conformation; D012545:Schiff Bases / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D014510:Urease / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism
chemical_list: D004791:Enzyme Inhibitors; D012545:Schiff Bases; D014510:Urease