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Updated: Mar 28, 2026

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
Published on: March 5, 2018
Eliminating caspase-7 and cathepsin B cross-reactivity on fluorogenic caspase-3 substrates
Martha Mackay1, Ana M Pérez-López1, Mark Bradley1
1EaStCHEM, School of Chemistry, University of Edinburgh, West Mains Road, EH9 3FJ Edinburgh, UK. annamaria.lilienkampf@ed.ac.uk mark.bradley@ed.ac.uk.
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)).

