Lecture: «Sugars Shapes & Peptide Folds: Synthetic Mimetics to Modulate Protein Function»
Prof. Dr. Aloysius Siriwardena (Laboratoire des Glycochimie, des Antimicrobiens et des Agroresources (CNRS) - Université de Picardie Jules Verne, Amiens, France)
Aula de Seminario del CiTIUS
12:15h
It is predicted that over half of all eukaryotic proteins are glycosylated and it is now established that co-and post-translational modification of proteins with glycans can have dramatic consequences on their folding, stability, and ultimately, their function.
Considerable effort has then not surprisingly been invested in delineating the impact of appended carbohydrates on the conformational preferences of proteins and peptides in solution and vice versa. It has been shown that important insights into the functioning of proteins and of glycopeptides can be gleaned from the study of carbohydrate mimetics and that the interactions of these mimetics with cellular targets can impact a wide range of physiological phenomena.
In this presentation we describe our efforts in the synthesis of a number mimetics designed as chemical probes with which to better understand protein-glycan interactions. We have been particularly interested in understanding using these, the interactions of glycans with their cognate receptors (lectins) as well as the modes-of-action (and modes-of-inhibition) of catalytic proteins (glycosidases and glycosyl transferases) responsible for the biosynthesis of glycans.