Literature

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.

DOI： 10.1016/j.ejmech.2011.09.009

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

European Journal of Medicinal Chemistry 2011.0

Synthesis and molecular docking study of some 5,6-dichloro-2-cyclopropyl-1 H -benzimidazole derivatives bearing triazole, oxadiazole, and imine functionalities as potent inhibitors of urease

Bioorganic & Medicinal Chemistry Letters 2017.0

Synthesis, molecular docking studies, and in vitro screening of sulfanilamide-thiourea hybrids as antimicrobial and urease inhibitors

Medicinal Chemistry Research 2013.0

Synthesis, biological evaluation, and molecular docking studies of 2,5-substituted-1,4-benzoquinone as novel urease inhibitors

Bioorganic & Medicinal Chemistry 2012.0

Design and synthesis of new barbituric- and thiobarbituric acid derivatives as potent urease inhibitors: Structure activity relationship and molecular modeling studies

Bioorganic & Medicinal Chemistry 2015.0

Synthesis of potent urease inhibitors based on disulfide scaffold and their molecular docking studies