Iron is an essential nutrient for growth and virulence for Pseudomonas aeruginosa, a multidrug resistant and nosocomial infection causing bacteria.Therefore, targeting the iron-regulated heme oxygenase (HemO) of Pseudomonas aeruginosa serves as a novel idea to overcome multidrug resistant infections. Here we present the synthesis and binding activity of a series of rhodanine-based inhibitors of HemO. This class of inhibitors acts by binding in the heme binding pocket site which is further supported by saturation transfer difference (STD) NMR as well as by heteronuclear single quantum coherence (HSQC) spectroscopy. An in vitro binding assay using fluorescence quenching was optimized to be automated for high throughput screening where one inhibitor, FX3028, showed a binding affinity of 3.3 μM. Further assays to test in cell activity as well as toxicity on this novel rhodanine family are currently being developed and optimized to be automated for high throughput screening to gather more supporting data.

Inhibition of the <i>Pseudomonas aeruginosa </i>heme oxygenase

254th National Meeting (2017)

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Inhibition of the Pseudomonas aeruginosa heme oxygenase