Glycosylation is the primary cause of micro-heterogeneity in proteins (glycoisoforms). These reflect complexity at both molecular and cellular levels. There are many potential functions of glycosylation. For instance, physical properties include: folding, trafficking, packing, stabilization, protease protection, quaternary structure and organization of water structure. Properties relating to recognition and biological triggering are characterized by: weak interactions, multiple presentation and precise geometry. Changes in sugar prints may both reflect and results in physiological changes, e.g. cancer and other diseases. Hence it is necessary to understand the degree of glycosylation. Furthermore, free glycans in human milk are known to stimulate the innate immune system of infants.
In this presentation an update about the latest technical developments of the Chip-MS system for glycan analysis will be provided. Applications of the Chip-MS system to the study of all classes of glycans (free glycans, N-glycans, O-glycans and glycosaminoglycans) will be discussed. Furthermore a method will be discussed that allows the determination of N-glycan, O-glycans and their glycosylation site in a single experiment including the analysis of stereo-glycopeptide isomers.