ArticleAnalytical chemistry2013
Time-resolved luminescence detection of spleen tyrosine kinase activity through terbium sensitization.
Article in Analytical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Clinical effect of spleen aminopeptide on improving liver function damage and immune function in children with infant hepatitis syndrome.World journal of gastrointestinal surgery · 2024Trial
- A Constellation of Fluorescent Biosensors to Illuminate the Galaxy of Protein Kinases.Chembiochem : a European journal of chemical biology · 2026Review
- Chemical synthesis of novel aminopyrimidin-4-yl-1H-pyrazole derivatives as spleen tyrosine kinase (SYK) inhibitors.Scientific reports · 2026Article
- Novel terbium-sensitizing peptide substrates for cyclin-dependent kinase 5 (CDK5) and their demonstration in luminescence kinase assays.RSC chemical biology · 2025Article
- Acetyl-Click Screening Platform Identifies Small-Molecule Inhibitors of Histone Acetyltransferase 1 (HAT1).Journal of medicinal chemistry · 2023Article
- De novo design of immunoglobulin-like domains.Nature communications · 2022Article
- Novel Bruton's Tyrosine Kinase (BTK) Substrates for Time-Resolved Luminescence Assays.ACS chemical biology · 2022Article
- Shining Light on Protein Kinase Biomarkers with Fluorescent Peptide Biosensors.Life (Basel, Switzerland) · 2022Review
- Phosphorylation-dependent protein design: design of a minimal protein kinase-inducible domain.Organic & biomolecular chemistry · 2019Article
- Redox-Responsive Protein Design: Design of a Small Protein Motif Dependent on Glutathionylation.Biochemistry · 2018Article
- Atomic force microscopy characterization of kinase-mediated phosphorylation of a peptide monolayer.Scientific reports · 2016Article
- Modular, Antibody-free Time-Resolved LRET Kinase Assay Enabled by Quantum Dots and Tb(3+)-sensitizing Peptides.Scientific reports · 2016Article
- Coupling the folding of a β-hairpin with chelation-enhanced luminescence of Tb(III) and Eu(III) ions for specific sensing of a viral RNA.Chemical science · 2016Article
- Selective Sensing of Tyrosine Phosphorylation in Peptides Using Terbium(III) Complexes.International journal of analytical chemistry · 2016Review
- Multicolored, Tb³⁺-Based Antibody-Free Detection of Multiple Tyrosine Kinase Activities.Analytical chemistry · 2015Article
- Integrating proteomics with electrochemistry for identifying kinase biomarkers.Chemical science · 2015Article
- KINATEST-ID: a pipeline to develop phosphorylation-dependent terbium sensitizing kinase assays.Journal of the American Chemical Society · 2015Article
- A time-resolved luminescence biosensor assay for anaplastic lymphoma kinase (ALK) activity.Chemical communications (Cambridge, England) · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Disruption of regulatory protein phosphorylation can lead to disease and is particularly prevalent in cancers. Inhibitors that target deregulated kinases are therefore a major focus of chemotherapeutic development. Achieving sensitivity and specificity in high-throughput compatible kinase assays is key to successful inhibitor development. Here, we describe the application of time-resolved luminescence detection to the direct sensing of spleen tyrosine kinase (Syk) activity and inhibition using a novel peptide substrate. Chelation and luminescence sensitization of Tb(3+) allowed the direct detection of peptide phosphorylation without any antibodies or other labeling reagents. Characterizing the Tb(3+) coordination properties of the phosphorylated vs unphosphorylated form of the peptide revealed that an inner-sphere water was displaced upon phosphorylation, which likely was responsible for both enhancing the luminescence intensity and also extending the lifetime, which enabled gating of the luminescence signal to improve the dynamic range. Furthermore, a shift in the optimal absorbance maximum for excitation was observed, from 275 nm (for the unphosphorylated tyrosine peptide) to 266 nm (for the phosphorylated tyrosine peptide). Accordingly, time-resolved measurements with excitation at 266 nm via a monochromator enabled a 16-fold improvement in base signal-to-noise for distinguishing phosphopeptide from unphosphorylated peptide. This led to a high degree of sensitivity and quantitative reproducibility, demonstrating the amenability of this method to both research laboratory and high-throughput applications.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.