NMR Study of Glycan Interactions Using Synthetic Oligosaccharides

Abstract

Recent advances in synthesizing methodologies and purification techniques significantly increase the accessibility of the major glycan structures, which are heterogeneously present on the glycoproteins and glycolipids. In contrast, it is often difficult to obtain sufficient amounts of minor structures consisting of a number of sugar units with reasonable purity sufficient for biological studies. In terms of the accessibility of the desired glycan sequences, it is useful in certain instances to deal with not the full sequence but with the required oligosaccharides, called glycan epitopes. Glycan epitopes have been used for the structural and functional analysis of the proteins that recognize particular glycans. For instance, lectins usually recognize the glycan epitope of a few sugar units, not in a “key-and-keyhole” manner but in a “pattern recognition receptor” mode. Such oligosaccharide epitopes can be prepared through regular chemical synthesis. This report describes recent progress on the NMR analysis of glycan–glycan and protein–glycan interactions using chemically synthesized glycan epitopes.