Dual-Mechanism Quenched Fluorogenic Probe Provides Selective and Rapid Detection of Cathepsin L Activity*
| Autor: | Ben Fetrow, Lina Cui, Biwu Ma, Jun Liu, Maya Chaaban, Peter Zannes Fatland, Kelton A. Schleyer |
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| Rok vydání: | 2020 |
| Předmět: |
Cathepsin L
chemical and pharmacologic phenomena 01 natural sciences Biochemistry Dual mechanism Rapid detection Article Drug Discovery Humans General Pharmacology Toxicology and Pharmaceutics Density Functional Theory Fluorescent Dyes Pharmacology Cathepsin chemistry.chemical_classification biology Molecular Structure 010405 organic chemistry Organic Chemistry hemic and immune systems Cysteine protease 0104 chemical sciences 010404 medicinal & biomolecular chemistry CTL Enzyme chemistry biology.protein Biophysics Molecular Medicine Selectivity |
| Zdroj: | ChemMedChem |
| ISSN: | 1860-7187 |
| Popis: | Cathepsin L (CTL) is a cysteine protease demonstrating upregulated activity in many disease states. Overlapping substrate specificity makes selective detection of CTL activity difficult to parse from that of its close homologue CTV and the ubiquitous CTB. Current probes of CTL activity have limited applications due to either poor contrast or extra assay steps required to achieve selectivity. We have developed a fluorogenic probe, CTLAP, that displays good selectivity for CTL over CTB and CTV while exhibiting low background fluorescence attributed to dual quenching mechanisms. CTLAP achieves optimum CTL selectivity in the first 10 min of incubation, thus suggesting that it is amenable for rapid detection of CTL, even in the presence of competing cathepsins. |
| Databáze: | OpenAIRE |
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