ArticleProceedings of the National Academy of Sciences of the United States of America2004
Metal ion-mediated polymer superquenching for highly sensitive detection of kinase and phosphatase activities.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Biosensors with Metal Ion-Phosphate Chelation Interaction for Molecular Recognition.Molecules (Basel, Switzerland) · 2023Review
- Parallel folding topology-selective label-free detection and monitoring of conformational and topological changes of different G-quadruplex DNAs by emission spectral changesChemical science · 2016Article
- Stochastic detection of Pim protein kinases reveals electrostatically enhanced association of a peptide substrate.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Identification and expression analysis of CjLTI, a novel low temperature responsive gene from Caragana jubata.Molecular biology reports · 2012Article
- Controlled aggregation in conjugated polymer nanoparticles via organic acid treatments.Macromolecules · 2011Article
- Biomimetic silica microspheres in biosensing.Molecules (Basel, Switzerland) · 2010Review
- Current Screens Based on the AlphaScreen Technology for Deciphering Cell Signalling Pathways.Current genomics · 2009Article
- Encapsulation of semiconducting polymers in vault protein cages.Nano letters · 2008Article
- High-throughput kinase assays with protein substrates using fluorescent polymer superquenching.BMC biotechnology · 2005Article
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Authors and funding
8 authors.
Funding
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Abstract
An assay technology for high-throughput screening of kinase and phosphatase activities is introduced. The format is based upon superquenching of fluorescent-conjugated polymers by dye-labeled kinase/phosphatase peptide substrates. The sensor platform is composed of highly fluorescent-conjugated polyelectrolytes colocated with the phosphate coordinating metal ion gallium on microspheres. Phosphorylated peptide substrates containing a quencher bind specifically to the metal ions by means of phosphate groups, resulting in quench of polymer fluorescence. The modulation of fluorescence signal is proportional to kinase or phosphatase activity and is monitored as a turn-off or turn-on signal, respectively. The assay is homogeneous and simple and can be run either as an endpoint measurement or in a kinetic mode. The assay meets the sensitivity required for high-throughput screening of kinase or phosphatase inhibitors and is a valuable tool for drug discovery. A modified version of the assay allows for the detection of protein phosphorylation.
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