The glycome is the entire set of sugars in a cell, tissue or organism at a certain time, including free and complex forms. Unlike genomes, the glycome is highly dynamic, due to the interplay of those more than 600 enzymes that can be involved in the complex pathways of protein glycosylation. In addition, glycosylation is cell, protein and site specific and epigenetic factors regulating the expression of glycosyltransferases and glycosidases may represent further diversifying mechanisms, influencing the functions of the proteins to which carbohydrates are attached. In the biomedical field, altered glycosylation is frequently associated with pathological conditions. Glycosylation modulation in the biotechnology industry, usually due to changes in bioprocessing/cell culture conditions, may alter the affectivity of biotherapeutics. In both instances, information about specific glycosylation motifs such as the type and number of sugar monomers along with their position and linkage specificity are of high importance. Glycomics, as a subset of glycobiology, systematically studies all glycan structures in a given sample. To fulfill the need of such global glycomics studies, automated, high throughput (preferably in 96 well plate formats) and robust bioanalytical platforms are required to address sample preparation (glycoprotein capture, glycan release and carbohydrate labeling), separation (capillary electrophoresis or liquid chromatography) and data processing (glycoinformatics) issues. This talk will confer the state of the art of analytical glycomics and discuss recent efforts and future prospective of this emerging field in regards to system integration, translational options and their implications in the biomedical and biopharmaceutical arena.
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