Abstract
Glycosylation is one of the structurally diverse and complex forms of post translational modifications observed in proteins which influence the effector functions of IgG-Fc. Although the glycosylation constitutes 2–3% of the total mass of the IgG antibody, a thorough assessment of glycoform distribution present on the antibody is a critical quality attribute (cQA) for the majority of novel and biosimilar monoclonal antibody (mAb) development. This review paper will highlight the impact of different glycoforms such as galactose, fucose, high mannose, NANA (N-acetylneuraminic acid), and NGNA (N-glycoylneuraminic acid) on the safety/immunogeneicity, efficacy/biological activity and clearance (pharmacodynamics/pharmacokinetic property (PD/PK)) of biological molecules. In addition, this paper will summarize routinely employed reliable analytical techniques such as hydrophilic interaction chromatography (HILIC), high performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD) and mass spectrometry (MS) for characterizing and monitoring glycosylation in monoclonal antibodies (mAbs). The advantages and disadvantages of each of the methods are addressed. The scope of this review paper is limited to only N-linked and O-linked glycosylation.
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