Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1804, Issue 3, Pages 541-546Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2009.10.019
Keywords
Protein kinase; Bisubstrate inhibitor; Fluorescent probe; Biosensor; ARC; Binding assay; Fluorescence anisotropy; Fluorescence polarization; FRET; SPR; HTS
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Conjugates of adenosine mimics and D-arginine-rich peptides (ARCs) are potent inhibitors of protein kinases (PKs) from the AGC group. Labeling ARCs with fluorescent dyes or immobilizing on chip surfaces gives fluorescent probes (ARC-Photo) and biosensors that can be used for high-throughput screening (HTS) of inhibitors of protein kinases. The bisubstrate character (simultaneous association with both binding sites of the kinase) and high affinity of ARCs allow ARC-based probes and sensors to be used for characterization of inhibitors targeted to either binding site of the kinase with affinities in whole nanomolar to micromolar range. The ability to penetrate cell plasma membrane and bind to the target kinase fused with a fluorescent protein leads to the possibility to use ARC-Photo probes for high content screening (HCS) of inhibitors in cellular milieu with detection of intensity of Forster resonance energy transfer (FRET) between two fluorophores. (C) 2009 Elsevier B.V. All rights reserved.
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