rifampin and nitrocefin

rifampin has been researched along with nitrocefin* in 2 studies

Other Studies

2 other study(ies) available for rifampin and nitrocefin

ArticleYear
Novel Piperazine Arylideneimidazolones Inhibit the AcrAB-TolC Pump in Escherichia coli and Simultaneously Act as Fluorescent Membrane Probes in a Combined Real-Time Influx and Efflux Assay.
    Antimicrobial agents and chemotherapy, 2016, Volume: 60, Issue:4

    In this study, we tested five compounds belonging to a novel series of piperazine arylideneimidazolones for the ability to inhibit the AcrAB-TolC efflux pump. The biphenylmethylene derivative (BM-19) and the fluorenylmethylene derivative (BM-38) were found to possess the strongest efflux pump inhibitor (EPI) activities in the AcrAB-TolC-overproducingEscherichia colistrain 3-AG100, whereas BM-9, BM-27, and BM-36 had no activity at concentrations of up to 50 μM in a Nile red efflux assay. MIC microdilution assays demonstrated that BM-19 at 1/4 MIC (intrinsic MIC, 200 μM) was able to reduce the MICs of levofloxacin, oxacillin, linezolid, and clarithromycin 8-fold. BM-38 at 1/4 MIC (intrinsic MIC, 100 μM) was able to reduce only the MICs of oxacillin and linezolid (2-fold). Both compounds markedly reduced the MIC of rifampin (BM-19, 32-fold; and BM-38, 4-fold), which is suggestive of permeabilization of the outer membrane as an additional mechanism of action. Nitrocefin hydrolysis assays demonstrated that in addition to their EPI activity, both compounds were in fact weak permeabilizers of the outer membrane. Moreover, it was found that BM-19, BM-27, BM-36, and BM-38 acted as near-infrared-emitting fluorescent membrane probes, which allowed for their use in a combined influx and efflux assay and thus for tracking of the transport of an EPI across the outer membrane by an efflux pump in real time. The EPIs BM-38 and BM-19 displayed the most rapid influx of all compounds, whereas BM-27, which did not act as an EPI, showed the slowest influx.

    Topics: Anti-Bacterial Agents; Bacterial Outer Membrane Proteins; Biological Assay; Biological Transport; Cell Membrane; Cephalosporins; Clarithromycin; Drug Synergism; Escherichia coli; Escherichia coli Proteins; Fluorescent Dyes; Gene Expression; Imidazoles; Indicators and Reagents; Kinetics; Levofloxacin; Linezolid; Membrane Proteins; Membrane Transport Proteins; Microbial Sensitivity Tests; Oxacillin; Piperazines; Protein Kinases; Repressor Proteins; Rifampin

2016
The effect of oligolysines Lys-3, Lys-4, and Lys-5 on the outer membrane permeability of Pseudomonas aeruginosa.
    FEMS microbiology letters, 1990, Jan-15, Volume: 55, Issue:1-2

    A lysine polymer with five residues (Lys-5) was found to remarkably increase the outer membrane (OM) permeability of Pseudomonas aeruginosa to the tested hydrophobic probes (nitrocefin, N-phenyl naphthylamine, rifampin). Lys-3 and Lys-4 were inactive. The OM of Escherichia coli and Salmonella typhimurium was not permeabilized by Lys-5. Furthermore, even the action of Lys-5 on the Pseudomonas OM was abolished when the assays were performed in the presence of 150 mM NaCl instead of the low-ionic strength buffer earlier used by investigators studying the effect of polycations on the Pseudomonas OM.

    Topics: 1-Naphthylamine; Cell Membrane Permeability; Cephalosporins; Fluorescent Dyes; Lipopolysaccharides; Osmolar Concentration; Polyamines; Polyelectrolytes; Polylysine; Polymers; Pseudomonas aeruginosa; Rifampin

1990