The central dogma of molecular biology has been that biological information moves from DNA to RNA to protein. However, there is a growing appreciation that posttranslational modifications, such as protein glycosylation, dramatically increase protein complexity and function.
Glycans are chains of monosaccharides that are covalently linked to cell surface proteins. They have been recognized as key participants in cell-cell communications. From a pathological point of view, changes in the glycome of cells are associated with developmental disorders and can mark the onset of cancer.
Despite these intriguing observations, the molecular mechanisms by which these complex carbohydrates influence cells are not well understood due to their inherent structural complexity and a lack of suitable biochemical methods to study them. To address these limitations, our research group focusses on two major lines of research:
- Development of fluorogenic bioorthogonal chemistry and probes in order to image glycans in living cells
- Probing and controlling the biosynthesis of glycans
Selected publications:
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Favre, C.; Friscourt, F.* Org. Lett. 2018, 20, 4213-4217.
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Chinoy, Z. S.; Bodineau, C.; Favre, C.; Moremen, K. W.; Durán R. V.; Friscourt, F.* Angew. Chem. Int. Ed. 2019, 58, 4281-4285
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Chinoy, Z. S.; Montembault, E.; Moremen, K. W.; Royou, A. and Friscourt, F.* ACS Chem. Biol. 2021, 16, 2307-2314.
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Chinoy, Z. S.; Moremen, K. W. and Friscourt, F.* Eur. J. Org. Chem. 2022, 27, e202200271.