Groupe de Recherche Cecioni Glycochimie et Glycomique chimique
Groupe de Recherche Cecioni

Our Research

Our group develops chemical tools to facilitate discoveries in the field of glycoscience. Our research relies on multidisciplinary approaches that encompass chemistry (organic synthesis, glycochemistry), biochemistry (enzyme kinetics, protein engineering, affinity characterization) as well as glycobiology (quantitative biology in live cells, glycome alterations).

We aim to develop chemical strategies that can be deployed in a physiologically relevant environment to (1) facilitate the study of glycan-protein interactions, (2) better understand the regulation of glycan-processing enzymes and (3) shed light on glycome dynamics in diseases.

Our long-term goal is to introduce research tools that are useful to the wider community of glyco-scientists and that can be exploited to accelerate both basic and translational research, for example through technologies for diagnostics or the discovery of pharmacological modulators of glycan-mediated processes.

Chemical biology to profile glycan-protein interactions

Dissecting glycan-protein interactions in their physiologically relevant environment remains highly challenging. For many important glycan-binding proteins (lectins), endogenous glycoconjugate ligands remain unknown. Furthermore, the existence of yet unknown mammalian glycan-binding domains (GBD) is a topic of high interest. 

Current approaches are limited in their ability to capture and to profile glycan-lectin interactions in live cells. Our group develops chemical probes and biochemical strategies that could help address these limitations. We synthesize and exploit proteomic probes as well as photochemical reporters in order to deliver complementary techniques that can be used on cultured cells and in tissues.

Chemical probes of glycan-processing enzymes

Within cells, a dynamic network of glycan-processing enzymes is responsible for creating, maintaining and recycling glycans. A number of theses enzymes have been proposed as therapeutic targets either through inhibition of their action or through pharmacological stabilization. 

Using chemical biology concepts, we work on molecules that enable quantitative monitoring of endogenous enzyme activity in live cells. These are important tools for discovering efficient inhibitors, but they will also ultimately help us clarify the roles of certain glyco-enzymes in human diseases. 

Chemical tools for perturbing glycan-protein interactions

The panel of available chemical modulators of glycan-lectin binding is relatively scarce, even for promising clinical targets. We are working at the design, screening and synthesis of small-molecule glycomimetics to perturb glycan-protein interactions. Notably, the identification of direct antagonists of non-covalent binding could have important translational potential but would also be useful to understand the role of a specific interaction in living systems. In addition, indirect alteration of glycan chemical structures can also perturb the glycan-binding recognition and these approaches constitute important tools for basic research.