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Séminaire Chimie IBMM

Chemical biology tools to perceive and perturb carbohydrates and carbohydrate processing enzymes in living systems

Prof. David Vocadlo (Departments of Chemistry and Molecular Biology Biochemistry, Simon Fraser University, Vancouver, Canada)

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Le Lundi 11 décembre 2017 à 14h
ENSCM, amphithéâtre Godechot (campus Balard, 240 av. Émile-Jeanbrau)

The carbohydrate structures found in every kingdom of life are emerging as a frontier area of chemical biology. We will discuss our work on the creation of new chemical biology tools for studying these structures and the enzymes that process them within cells and in animal models, with a particular view to understanding and combating neurodegenerative diseases. Topics will be selected from the synthesis and deployment of : (i) a new family of fluorescence-quenched substrates that permit quantitative imaging of glycoside hydrolase activities in live cells by high content imaging, (ii) the design, synthesis, and creation of potent and selective inhibitors of carbohydrate processing enzymes active in cells and in vivo, and (iii) new chemical genetic methods to map glycosylation to the genome.

Selected recent publications

S. Cecioni, D.J. Vocadlo, Carbohydrate bis-acetal-based substrates as tunable fluorescence-quenched probes for monitoring exo-glycosidase activity. J. Am. Chem. Soc. 2017, 139, 8392.
C. Roth, et al, Structural and functional insight into human O-GlcNAcase. Nat. Chem. Biol. 2017, 13, 610.
T.-W. Liu, et al, Genome-wide chemical mapping of O-GlcNAcylated proteins in Drosophila melanogaster. Nat. Chem. Biol. 2017, 13, 161.
G.E. Perley-Robertson, et al, A fluorescent transport assay enables studying AmpG permeases involved in peptidoglycan recycling and antibiotic resistance. ACS Chem. Biol. 2016, 11, 2626.
N. Cekic, et al, Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human O-GlcNAcase. Chem. Sci. 2016, 7, 3742.
M. Bergeron-Brlek, et al, Angew. Chem. Int. Ed. 2015, 54, 15429.

Contact local IBMM : Dr. Muriel Amblard, D.R. CNRS / Dr. Lubomir Vezenkov (DAPP)

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