Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10533719 | Analytical Biochemistry | 2012 | 5 Pages |
Abstract
An electrochemical method based on the bioorganometallic Fc-ATP cosubstrate for kinase-catalyzed phosphorylation reactions was used for monitoring casein kinase 2 (CK2) phosphorylations in the absence and presence of five indole/quinolone-based potential inhibitors. Fc-phosphorylation of immobilized peptide RRRDDDSDDD on Au surfaces resulted in a current density at approximately 460 ± 10 mV. An electrochemical redox signal was significantly decreased in the presence of inhibitors. In addition, the electrochemical signal was concentration dependent with respect to the potential inhibitors 1 to 5, which proved to be viable CK2 drug targets with estimated IC50 values in the nanomolar range.
Related Topics
Physical Sciences and Engineering
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Analytical Chemistry
Authors
Sanela MartiÄ, Stefanie Tackenburg, Yaroslav Bilokin, Andriy Golub, Volodymyr Bdzhola, Sergiy Yarmoluk, Heinz-Bernhard Kraatz,