Autor: |
Ana M Pérez-López, M Lourdes Soria-Gila, Emma R Marsden, Annamaria Lilienkampf, Mark Bradley |
Jazyk: |
angličtina |
Rok vydání: |
2016 |
Předmět: |
|
Zdroj: |
PLoS ONE, Vol 11, Iss 5, p e0153209 (2016) |
Druh dokumentu: |
article |
ISSN: |
1932-6203 |
DOI: |
10.1371/journal.pone.0153209 |
Popis: |
The in situ detection of caspase-3 activity has applications in the imaging and monitoring of multiple pathologies, notably cancer. A series of cell penetrating FRET-based fluorogenic substrates were designed and synthesised for the detection of caspase-3 in live cells. A variety of modifications of the classical caspase-3 and caspase-7 substrate sequence Asp-Glu-Val-Asp were carried out in order to increase caspase-3 affinity and eliminate caspase-7 cross-reactivity. To allow cellular uptake and good solubility, the substrates were conjugated to a cationic peptoid. The most selective fluorogenic substrate 27, FAM-Ahx-Asp-Leu-Pro-Asp-Lys(MR)-Ahx, conjugated to the cell penetrating peptoid at the C-terminus, was able to detect and quantify caspase-3 activity in apoptotic cells without cross-reactivity by caspase-7. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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