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Research Article

Inhibition of Bacillus anthracis metallo-β-lactamase by compounds with hydroxamic acid functionality

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Pages 132-137 | Received 24 Mar 2016, Accepted 20 Jul 2016, Published online: 25 Aug 2016

Figures & data

Figure 1. Schemes of the syntheses of hydroxymate-containing compounds. (A) The scheme of the synthesis of 3-(heptyloxy)-N-hydroxybenzamide (compound 4). (B) The scheme of the synthesis of N-hydroxy-3-((6-(hydroxyamino)-6-oxohexyl)oxy)benzamide (compound 7).

Figure 1. Schemes of the syntheses of hydroxymate-containing compounds. (A) The scheme of the synthesis of 3-(heptyloxy)-N-hydroxybenzamide (compound 4). (B) The scheme of the synthesis of N-hydroxy-3-((6-(hydroxyamino)-6-oxohexyl)oxy)benzamide (compound 7).

Figure 2. Concentration–response plots for Bla2 inhibition with compound 7.

Figure 2. Concentration–response plots for Bla2 inhibition with compound 7.

Figure 3. Lineweaver–Burke plots of inhibition of Bla2 y compound 7. The concentrations of compound 7 are 0 (circle), 0.5 (square), and 1.0 μM (triangle). Assays were performed in 50 mM MOPS, pH 7.0. Kinetic constants were determined by fitting of the data to the equation v = VmaxS/[Km·(1 + 1/Ki) + S] which indicates competitive inhibition.

Figure 3. Lineweaver–Burke plots of inhibition of Bla2 y compound 7. The concentrations of compound 7 are 0 (circle), 0.5 (square), and 1.0 μM (triangle). Assays were performed in 50 mM MOPS, pH 7.0. Kinetic constants were determined by fitting of the data to the equation v = VmaxS/[Km·(1 + 1/Ki) + S] which indicates competitive inhibition.

Figure 4. Molecular docking between Bla2 and the compounds (4 and 7). (A and B) A snapshot of binding mode of compound 7 and Bla2. (C and D) A snapshot of binding mode of compound 4 and Bla2.

Figure 4. Molecular docking between Bla2 and the compounds (4 and 7). (A and B) A snapshot of binding mode of compound 7 and Bla2. (C and D) A snapshot of binding mode of compound 4 and Bla2.
Supplemental material

IENZ_1222580_Supplementary_Material.pdf

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