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Chem Biol ; 11(4): 499-508, 2004 Apr.
Article in English | MEDLINE | ID: mdl-15123244

ABSTRACT

Two molecular sensors that specifically recognize ADP in a background of over 100-fold molar excess of ATP are described. These sensors are nucleic-acid based and comprise a general method for monitoring protein kinase activity. The ADP-aptamer scintillation proximity assay is configured in a single-step, homogeneous format while the allosteric ribozyme (RiboReporter) sensor generates a fluorescent signal upon ADP-dependent ribozyme self-cleavage. Both systems perform well when configured for high-throughput screening and have been used to rediscover a known protein kinase inhibitor in a high-throughput screening format.


Subject(s)
Adenosine Diphosphate/analysis , Adenosine Diphosphate/metabolism , Biosensing Techniques/methods , Protein Kinases/analysis , Protein Kinases/metabolism , Adenosine Triphosphate/metabolism , Base Sequence , Fluorescence , Ligands , Molecular Sequence Data , RNA, Catalytic/chemistry , RNA, Catalytic/metabolism , Signal Transduction , Substrate Specificity , Time Factors
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