ArticleRSC advances2025
A new multi-purpose FRET fluorescent probe for the simultaneous detection of proteases.
Article in RSC advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Authors and funding
5 authors.
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Abstract
A new methodology for the detection of three model proteases using a multi-purpose peptide probe equipped with three selectively cleavable sites and four fluorophores was developed and studied. The probe was designed as a single-excitation, triple-emission system, allowing for the monitoring of characteristic real-time changes in the fluorescence emission responses of individual fluorophores during enzymatic cleavage. It was labelled with diethylaminocoumarin (DEAC), fluorescein (FL) and Rhodamine B (RhB), forming the DEAC → FL → RhB FRET-cascade, with estimated Förster distances of 3.08 ± 0.02 nm or 3.02 ± 0.02 nm for the DEAC → FL FRET-pair (depending on the DEAC labeling site) and 6.04 ± 0.05 nm for the FL → RhB FRET-pair. Although spectroscopic analyses indicate that photophysical processes other than FRET are involved in the probe, the huge changes in its fluorescence intensities (
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