Proteins carry out pivotal functions in cells. Less appreciated is that the proteins are sugar coated and that glycosylation affects how the immune system recognizes the protein, as being friend or foe. Unlike proteomics, glycomics is not identified by structures and sequence of the single units is not predefined. This makes difficult and tricky the study of glycosylation and glycoproteomics. However, the role of glycome code on cellular mechanisms cannot be neglected. Glycosylation of proteins is a major event in posttranslational processing along their route, cell surface proteins are mainly glycoproteins. Hence, glycosylation changes and glycan-protein interactions feature malignant transformation and tumor progression. The distance between glycomics and proteomics is still far and it is missed the methodological approach to pinpoint the site where glycosylation takes place.
Here, glycomics and glycoproteomics are analyzed and the role that microfluidics can play in research is investigated by the description of the already reported application. The margins of improvement of microfluidics are still wide. Here, analyzing the structural hierarchical levels, we intend critically discuss the role that microfluidics might have in boosting knowledge and progress in glycoscience.