Synthesis, biological assay in vitro and molecular docking studies of new Schiff base derivatives as potential urease inhibitors

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 mu M) and 3k (K-i = 0.122 mu M). 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. (C) 2011 Elsevier Masson SAS. All rights reserved.