Abstract
Responsive ARC-Lum probes were used for measurement of the concentration of active protein kinases (PKs) and determination of affinity of inhibitors of PKs. ARC-Lum probes incorporate thiophene or a selenophene heterocycle and a fluorophore conjugated to the lysine residue in the peptide fragment. In the complex with a PK, ARC-Lum probes emit long-lifetime (microsecond-scale) luminescence at the emission wavelengths of the fluorescent label if the complex is illuminated at the excitation wavelength of the thiophene- or selenophene-containing phosphorescence donors. Bisubstrate ARC-Lum probes bind with sub-nanomolar affinity with several PKs of the AGC group. This article is part of a Special Issue entitled: Inhibitors of Protein Kinases (2012).
Copyright © 2013 Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Algorithms
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Anisotropy
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Binding Sites
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Binding, Competitive
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Biocatalysis / drug effects
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Fluorescent Dyes / chemistry
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Fluorescent Dyes / metabolism*
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Kinetics
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Lysine / chemistry
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Lysine / metabolism*
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Models, Chemical
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Molecular Structure
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Protein Binding
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Protein Kinase C / antagonists & inhibitors
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Protein Kinase C / chemistry
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Protein Kinase C / metabolism
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Protein Kinase Inhibitors / metabolism*
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Protein Kinase Inhibitors / pharmacology
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Protein Kinases / chemistry
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Protein Kinases / metabolism*
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Spectrophotometry
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Staurosporine / metabolism
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Staurosporine / pharmacology
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Thiophenes / chemistry
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Thiophenes / metabolism
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Time Factors
Substances
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Fluorescent Dyes
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Protein Kinase Inhibitors
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Thiophenes
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Protein Kinases
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Protein Kinase C
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Staurosporine
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Lysine