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A Selective, Dual Emission β-Alanine Aminopeptidase Activated Fluorescent Probe for the Detection of Pseudomonas aeruginosa, Burkholderia cepacia, and Serratia marcescens.


ABSTRACT: Selective detection of β-alanyl aminopeptidase (BAP)-producing Pseudomonas aeruginosa, Serratia marcescens, and Burkholderia cepacia was achieved by employing the blue-to-yellow fluorescent transition of a BAP-specific enzyme substrate, 3-hydroxy-2-(p-dimethylaminophenyl)flavone derivative, incorporating a self-immolative linker to β-alanine. Upon cellular uptake and accumulation of the substrate by viable bacterial colonies, blue fluorescence was generated, while hydrolysis of the N-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.

SUBMITTER: Varadi L 

PROVIDER: S-EPMC6804094 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature

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A Selective, Dual Emission β-Alanine Aminopeptidase Activated Fluorescent Probe for the Detection of <i>Pseudomonas aeruginosa</i>, <i>Burkholderia cepacia</i>, and <i>Serratia marcescens</i>.

Váradi Linda L   Najib Elias Y EY   Hibbs David E DE   Perry John D JD   Groundwater Paul W PW  

Molecules (Basel, Switzerland) 20190930 19


Selective detection of β-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 β-alanine. Upon cellular uptake and accumulation of the substrate by viable bacterial colonies, blue fluorescence was generated, while hyd  ...[more]

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