Fig. 2: Potent inhibition by BWC0977 on gyrase supercoiling and topoisomerase IV decatenation activities. | Communications Biology

Fig. 2: Potent inhibition by BWC0977 on gyrase supercoiling and topoisomerase IV decatenation activities.

From: Structural interactions of BWC0977 with Klebsiella pneumoniae topoisomerase IV and biochemical basis of its broad-spectrum activity

Fig. 2: Potent inhibition by BWC0977 on gyrase supercoiling and topoisomerase IV decatenation activities.

The graphs illustrate the inhibition potency of BWC0977 compared to ciprofloxacin on the DNA supercoiling activity of gyrases and the decatenation activity of topoisomerase IV from A E. coli, B P. aeruginosa and C S. aureus. The IC50 values were calculated using appropriate reaction controls; maximum reaction (no compound, 100% enzyme activity) and minimum reaction (no enzyme, 0% enzyme activity). The error bars in the plots represent the standard deviation of three E. coli and S. aureus or two P. aeruginosa independent experiments. BWC0977 induces single strand breaks mediated by gyrase and topoisomerase IV. The gel images show BWC0977 concentration response (μM) performed with D E. coli gyrase and E E. coli topoisomerase IV in a DNA cleavage assay setup. The gel bands (L = linear DNA, N = nicked DNA, C = circular DNA) were quantified and plotted on GraphPad Prism as % DNA breaks induced by BWC0977 with F gyrase and G topoisomerase IV enzymes. The error bars represent the standard deviation of three independent experiments.

Back to article page