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Kinase-templated abiotic reaction† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c7sc01416c Click here for additional data file.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Saarbach, Jacques Lindberg, Eric Folliet, Sarah Georgeon, Sandrine Hantschel, Oliver Winssinger, Nicolas |
| Copyright Year | 2017 |
| Abstract | Protein kinases are quintessential regulators of cellular function. Numerous pathologies are intimately linked to the dysregulated activity of a particular protein kinase. Herein we report a technology based on a proximity-induced chemical transformation that enables the detection and imaging of specific kinases. Using two probes that target the nucleotide-binding site and substrate binding site of a target kinase respectively, the reagents appended on the probes are brought within reactive distance thereby enabling the chemical transformation. The reaction used for sensing is a ruthenium-photocatalyzed reduction of a pyridinium immolative linker, which uncages a fluorophore (rhodamine). We demonstrate that this technology can be used to discriminate between closely related kinases with a high signal to noise ratio. We further demonstrate that the technology operates within the complexity of a cellular context with a good correlation between the level of kinase activity and fluorescence output. |
| Starting Page | 5119 |
| Ending Page | 5125 |
| Page Count | 7 |
| File Format | PDF HTM / HTML |
| DOI | 10.1039/c7sc01416c |
| PubMed reference number | 28970898 |
| Journal | Medline |
| Volume Number | 8 |
| Alternate Webpage(s) | http://www.rsc.org/suppdata/c7/sc/c7sc01416c/c7sc01416c1.pdf |
| Alternate Webpage(s) | https://doi.org/10.1039/c7sc01416c |
| Journal | Chemical science |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |