CARB 3 |
| A majority of cell surface and secreted proteins are posttranslationally modified by the addition of glycans. These complex structures can provide information regarding the state of health of cells or organisms. Indeed, changes in the structures of protein- and cell surface-associated glycans are a hallmark of many cancers, chronically inflamed tissues, and microbial infections. The ability to probe glycosylation in living systems may therefore reveal new biomarkers of disease and provide new avenues for diagnostic imaging. We are developing chemical technologies for visualizing glycans in living systems. As products of secondary metabolism, glycans are constructed from simple monosaccharide precursors. We exploit these metabolic pathways to incorporate bioorthogonal chemical reporters into glycans. The chemical reporters comprise small functional groups, such as the azide, that can be detected by covalent reaction with highly selective probes. New chemical reactions have been developed for this purpose, such as the Staudinger ligation with phosphines and strain-promoted [3+2] cycloaddition with functionalized cyclooctynes. Applications of the technique to the identification of cancer-associated glycan biomarkers and noninvasive imaging are currently being pursued. |
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Claude S. Hudson Award in Carbohydrate Chemistry: Symposium in Honor of Pierre Sina˙
8:45 AM-12:10 PM, Sunday, March 25, 2007 McCormick Place North -- Room N226, Level 2, Oral
Division of Carbohydrate Chemistry |