Issue 64, 2016, Issue in Progress

β-Alanyl aminopeptidase-activated fluorogenic probes for the rapid identification of Pseudomonas aeruginosa in clinical samples

Abstract

The fluorogenic self-immolative substrates 8 are specifically hydrolyzed by β-alanyl aminopeptidase, resulting in a 1,6-elimination and the release of the highly fluorescent hydroxycoumarins 6. 7-{4-(β-Alanylamino)}benzyloxy-3-ethoxycarbonylcoumarin trifluoroacetate 8b has advantages over another fluorogenic substrate, 7-N-β-alanylamino-4-methylcoumarin 9, as it is retained by bacterial colonies in solid agar applications, and results in similar times to detection, stronger fluorescence intensities, and no decrease in signal over time in liquid media. Although 7-{4-(β-alanylamino)}benzyloxy-4-methylcoumarin trifluoroacetate 8a produces a weaker signal than substrate 8b, its use allowed better discrimination between the BAP producers P. aeruginosa (positive) and S. marcescens (negative).

Graphical abstract: β-Alanyl aminopeptidase-activated fluorogenic probes for the rapid identification of Pseudomonas aeruginosa in clinical samples

Supplementary files

Article information

Article type
Paper
Submitted
18 May 2016
Accepted
11 Jun 2016
First published
13 Jun 2016

RSC Adv., 2016,6, 58884-58889

Author version available

β-Alanyl aminopeptidase-activated fluorogenic probes for the rapid identification of Pseudomonas aeruginosa in clinical samples

L. Váradi, D. E. Hibbs, S. Orenga, M. Babolat, J. D. Perry and P. W. Groundwater, RSC Adv., 2016, 6, 58884 DOI: 10.1039/C6RA12875K

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