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>

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.

Keywords

• fluorescent probe
• <i>pseudomonas aeruginosa</i>
• bacterial detection
• self-immolative
• 3-hydroxyflavone