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


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 ?M KM values and good catalytic efficiencies (7.0-16.9 ?M(-1) min(-1)).

SUBMITTER: Mackay M 

PROVIDER: S-EPMC4763880 | biostudies-other | 2016 Mar

REPOSITORIES: biostudies-other

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

Mackay Martha M   Pérez-López Ana M AM   Bradley Mark M   Lilienkampf Annamaria A  

Molecular bioSystems 20160301 3


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)). ...[more]

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