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In order to study the various physiological functions of glycans, it is very essential to use a structurally defined oligosaccharide due to the structural diversity and heterogeneity that oligosaccharides impart on the post-translational modifications furnished in protein biosynthesis. Disialyloctasaccharide (1) and Sialylglycopeptide (2) are available as homogenous glycan donors for oligosaccharide remodeling reactions.1) Illustrative of this, heterogenous non-fucosylated N-glycans bound to therapeutic antibody are replaced by the structurally defined N-glycan by the oligosaccharide remodeling reaction of N-glycan with Glycosynthase (Endo-M-N175Q) which is an endo-β-N-Acetylglucosaminidase (Endo-M) mutant.
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