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

Martha Mackay; Ana Perez-Lopez; Mark Bradley; Annamaria Lilienkampf

doi:10.1039/c5mb00730e

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

Martha Mackay, Ana Perez-Lopez, Mark Bradley, Annamaria Lilienkampf

Research output: Contribution to journal › Article › peer-review

Abstract / Description of output

11 FRET-based fluorogenic substrates were constructed using the pentapeptide template Asp-Glu-X2-Asp-X10, 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 lM KM values and good catalytic efficiencies (7.0–16.9 lM 1 min 1).

Original language	English
Pages (from-to)	693-696
Journal	Molecular BioSystems
Volume	12
Issue number	3
DOIs	https://doi.org/10.1039/c5mb00730e
Publication status	Published - 12 Dec 2015

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title = "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-X10, 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 lM KM values and good catalytic efficiencies (7.0–16.9 lM 1 min 1).",

author = "Martha Mackay and Ana Perez-Lopez and Mark Bradley and Annamaria Lilienkampf",

year = "2015",

month = dec,

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doi = "10.1039/c5mb00730e",

language = "English",

volume = "12",

pages = "693--696",

journal = "Molecular BioSystems",

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publisher = "Royal Society of Chemistry",

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T1 - Eliminating caspase-7 and cathepsin B cross-reactivity on fluorogenic caspase-3 substrates

AU - Mackay, Martha

AU - Perez-Lopez, Ana

AU - Bradley, Mark

AU - Lilienkampf, Annamaria

PY - 2015/12/12

Y1 - 2015/12/12

N2 - 11 FRET-based fluorogenic substrates were constructed using the pentapeptide template Asp-Glu-X2-Asp-X10, 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 lM KM values and good catalytic efficiencies (7.0–16.9 lM 1 min 1).

AB - 11 FRET-based fluorogenic substrates were constructed using the pentapeptide template Asp-Glu-X2-Asp-X10, 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 lM KM values and good catalytic efficiencies (7.0–16.9 lM 1 min 1).

U2 - 10.1039/c5mb00730e

DO - 10.1039/c5mb00730e

M3 - Article

SN - 1742-2051

VL - 12

SP - 693

EP - 696

JO - Molecular BioSystems

JF - Molecular BioSystems

IS - 3

ER -

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

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