Abstract / Description of output
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.
Original language | English |
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Article number | 0153209 |
Number of pages | 11 |
Journal | PLoS ONE |
Volume | 11 |
Issue number | 5 |
DOIs | |
Publication status | Published - 11 May 2016 |
Keywords / Materials (for Non-textual outputs)
- ACTIVITY-BASED PROBES
- UNNATURAL AMINO-ACIDS
- PENETRATING PEPTIDES
- APOPTOTIC PATHWAYS
- CANCER
- SPECIFICITY
- CLEAVAGE
- INHIBITORS
- DISCOVERY
- PROTEASES