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Glycosylation is structurally the most complex posttranslational modification of proteins, playing key roles in many biological and disease processes. To understand the biology of glycans and glycoconjugates and to develop biologicals, it is essential to determine exact glycan structures.

This work describes new electrophoretic analysis approaches for the separation and identification of glycans, based on their mobility in the liquid and gas phase. An overview of CE for the analysis of glycans as well as proteins is given and a novel method, using CE-MS, is presented for sensitive glycan analysis. In this method, CE has been improved for sensitive glycan analysis using large volume injections with in-line sample trapping.

In addition, new ion mobility spectrometry (IMS)-MS approaches, developed using well-defined standards, are described for accurate structural assignment of glycans. These approaches enable exact glycan structure elucidation, without further need for standards, by measuring the intrinsic gas phase conformer distribution of intact and collision induced fragment ions with IMS-MS.

The developments described in this work, complement and enhance the current available analytical techniques, providing high sensitivity and distinct separation selectivity, with respect to LC, and improved exact glycan structure elucidation for their characterization in biological samples and biologicals.