ORGN 130 |
| Catalyzed by kinases, serine/threonine and tyrosoine phosphorylation is a vital mechanism of intracellular regulation. Thus, assays that easily monitor kinase activity are critical in both academic and pharmaceutical settings. We previously developed sulfonamido-oxine (Sox)-based fluorescent peptides following a linear design for the continuous assay of kinase activity in vitro and in cell lysates. Upon phosphorylation of the Sox-containing peptide, the chromophore complexes to Mg(II) and undergoes a chelation-enhanced fluorescence. While the design was applied successfully toward the development of multiple kinase sensors, one of the intrinsic limitations was that only residues on one side of the phosphorylated residue could be used to derive specificity for the target kinase. To address this issue, a new strategy has been developed, termed the branched design, that allows exploitation of the full substrate recognition sequence. This method now permits the construction of chemosensors with enhanced in vitro selectivity toward Aurora A and PKCα kinases.
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Total Synthesis, Materials, Devices and Switches, Molecular Recognition and Self-Assembly, Biologically-Related Molecules and Processes
8:00 PM-10:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Organic Chemistry |
