ORGN 667 |
| Reversible protein phosphorylation regulates diverse cellular processes including signal transduction, transcription, cell division and metabolic pathways. With the significance of phosphorylation, identification of phosphoproteins is important to understand biological functions. Since the current phosphopeptide enrichment methods are challenging, development of new isolation procedures is needed. Here direct phosphate modification of phosphopeptides and phosphoproteins using an oxidation-reduction condensation is shown as a method of phosphopeptide enrichment. To validate the selectivity, phosphopeptide containing phosphoserine, phosphothreonine and phosphotyrosine were isolated from a complex peptide mixture. Furthermore, the phosphopeptide enrichment method was applied to enrich phosphopeptides from a protein digestion and full length phosphoproteins from a cellular mixture, demonstrating its suitability for phosphoproteomics research. The oxidation reduction condensation method displays general reactivity towards phosphopeptides, high chemical selectivity and dependence on only commercially available reagents, making it a useful tool for phosphopeptide analysis and for development of new phosphoproteomics tools.
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Asymmetric Reactions, Combinatorial Chemistry, Molecular Recognition and Self-Assembly, Proteins, Peptides, Amino Acids and Enzyme Inhibitors
8:00 PM-10:00 PM, Wednesday, March 28, 2007 Hyatt Regency Chicago -- Riverside Center, Poster
Division of Organic Chemistry |
