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Selective detection of &#946;-alanyl aminopeptidase (BAP)-producing <i>Pseudomonas aeruginosa</i>, <i>Serratia marcescens</i>, and <i>Burkholderia cepacia</i> was achieved by employing the blue-to-yellow fluorescent transition of a BAP-specific enzyme substrate, 3-hydroxy-2-(<i>p</i>-dimethylaminophenyl)flavone derivative, incorporating a self-immolative linker to &#946;-alanine. Upon cellular uptake and accumulation of the substrate by viable bacterial colonies, blue fluorescence was generated, while hydrolysis of the <i>N</i>-terminal peptide bond by BAP resulted in the elimination of the self-immolative linker and the restoration of the original fluorescence of the flavone derivative.