Protein phosphorylation is a ubiquitous posttranslational modification that regulates cell signaling in both prokaryotes and eukaryotes. The dysregulation of kinases and phosphatases has been linked to many disease processes in humans, including cancer. Accordingly, protein kinases are important drug targets in the pharmaceutical industry. Kinases have recently been identified as potential drug targets in the search for antibacterial agents. Although the study of phosphorylated proteins has made great progress in the last decade, global phosphoproteomics studies are still challenges for several reasons, including the instability of the phospho-amino acid bonds and the low abundance of phosphoproteins. These issues are particularly exacerbated when examining phosphorylation at sites other than Ser, Thr and Tyr. To address these challenges, we are pursuing the development of a chemical method capable of specifically targeting phosphorylated amino acids in order to identify phosphoproteins from complex biological samples.

Chemical tools for the selective detection of phosphorylated proteins

244th National Meeting (2012)

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