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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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Publication details

The article was received on 30 Oct 2015, accepted on 07 Dec 2015 and first published on 08 Dec 2015


Article type: Communication
DOI: 10.1039/C5MB00730E
Citation: Mol. BioSyst., 2016,12, 693-696
  • Open access: Creative Commons BY license
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    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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