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Differentiation of α2,3 and α2,6 Sialic Acid Linked Glycan Isomers using SelexION Differential Mobility Spectrometry Technology

Protein glycosylation is one of the most common and yet most complex post-translational modifications, displaying diversity both in site occupancy and in glycan structure. Sialic acids are typically found at the outermost ends of glycan chains, and have important function in many physiological and pathological processes, including pathogen binding and regulation of the immune response. In human cells, the linkage position of a sialic acid to a glycan side chain can be α2,3 or α2,6 to a galactose residue, α2,6 to a N-acetylgalactosamine (GalNAc) residue, or α2,8 to another sialic acid residue. The linkage configuration has important consequences for biological function, for example, upregulation of α2,3 linked sialic acid is associated with metastasis progression in certain cancers. For the development of biopharmaceuticals, characterization of sialylation is essential for determination of function and efficacy.