Discovery and Study of the Binding Epitopes of Novel Urease Inhibitors by STD-NMR Spectroscopy and Biochemical Analyses
Bishnu P. Marasini,
M. Arif Lodhi,
M. Iqbal Choudhary.
In this study, Saturation Transfer Difference NMR (STD NMR) was employed for the first time to detect the
binding epitopes of new inhibitors of the enzyme urease. Inhibition of urease is recognized as an important approach towards
the treatment of ulcer, urolithiasis and related diseases. During the current study, STD-NMR was used as a tool for
the identification of structural features responsible for inhibition of urease enzyme at the atomic levels. This approach,
combined with mechanism-based biochemical assay, is specially suited for the discovery and optimization of potent inhibitors
of enzymes. Urease from Jack beans was used for epitope mapping of inhibitors, i.e. flavonoid glycosides, hypoxanthine
and benzodioxane derivatives and STD-NMR results were compared with the results of kinetic studies.
Keywords: Epitope mapping, Benzodioxane, Flavonoids, Hypoxanthine, Saturation Transfer Difference NMR, Urease
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