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Issue 3, 2016
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Eliminating caspase-7 and cathepsin B cross-reactivity on fluorogenic caspase-3 substrates

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Abstract

11 FRET-based fluorogenic substrates were constructed using the pentapeptide template Asp-Glu-X2-Asp-X1′, and evaluated with caspase-3, caspase-7 and cathepsin B. The sequence Asp-Glu-Pro-Asp-Ser was able to selectively quantify caspase-3 activity in vitro without notable caspase-7 and cathepsin B cross-reactivity, while exhibiting low μM KM values and good catalytic efficiencies (7.0–16.9 μM−1 min−1).

Graphical abstract: Eliminating caspase-7 and cathepsin B cross-reactivity on fluorogenic caspase-3 substrates

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Supplementary files

Article information


Submitted
30 Oct 2015
Accepted
07 Dec 2015
First published
08 Dec 2015

This article is Open Access

Mol. BioSyst., 2016,12, 693-696
Article type
Communication
Author version available

Eliminating caspase-7 and cathepsin B cross-reactivity on fluorogenic caspase-3 substrates

M. Mackay, A. M. Pérez-López, M. Bradley and A. Lilienkampf, Mol. BioSyst., 2016, 12, 693
DOI: 10.1039/C5MB00730E

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