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† Change of AHL quenching and proteolytic activity when PF-1240 was modified.Quenching of AHL quenching experiments were carried out by adding different amounts of PF-1240 to AiiA-treated AHLs (see Fig. 6). PF-1240 was added at different concentrations (1, 3, 6, 10, 15 and 20 μM) to the AHLs of different carbon chain lengths (C~6~, C~8~, C~10~, C~12~, C~14~, C~16~, C~18~ and C~20~). After incubation for 30 min at room temperature, the proteolytic activity of AiiA (1 μM) was assessed. The proteolytic activity was quantified by measuring the fluorescence intensity (400/500 nm) of the released AmiC-His~6~. (**A**) Proteolytic activity of AiiA (1 μM) in the presence of PF-1240 (1, 3, 6, 10, 15 and 20 μM). (**B**) Quenching of C~10~-AHL by PF-1240 (10 μM). The quenching of AHLs by PF-1240 has been calculated from the fluorescence changes (at 400/500 nm) in the presence of PF-1240. The values represent the mean ± SD (*n* = 3). PF-1240 was added at various concentrations (1, 3, 6, 10, 15 and 20 μM). The AHLs were prepared in DMSO and used at a final concentration of 50 μM. (**C**) Proteolytic activity of AiiA (1 μM) in the presence of cycloheximide (CHX) or proteinase K. Proteolytic activity was assessed by measuring the fluorescence intensity (400/500 nm) of the released AmiC-His~6~. CHX or proteinase K (50 μg/mL) was added to the reaction at 30-min intervals. The values represent the mean ± SD (*n* = 3). The reaction (AiiA and AHLs) was started by adding the protease inhibitor at time zero. The proteolytic activity of AiiA (1 μM) in the presence of PF-1240 (10 μM) was assessed by measuring the fluorescence intensity (

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