ReviewAdvances in experimental medicine and biology2026
Glycan Remodeling Technologies for Enhancing Antibody Function.
Review in Advances in experimental medicine and biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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2 authors.
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Abstract
Antibodies have become a major class of medicines, with over 60 therapeutic antibodies currently approved for clinical use. Immunoglobulin G (IgG) contains N-linked glycans in its Fc domain, which play a crucial role in functions such as antibody-dependent cellular cytotoxicity (ADCC) and pharmacokinetics. Profiling N-linked glycans is essential for antibody drug development, quality control, and biosimilar production. However, glycan structures are highly heterogeneous due to complex biosynthetic pathways, leading to batch-to-batch variations that impact antibody efficacy and safety. Recent advancements in mass spectrometry and chromatography have enabled more precise structural analysis of N-linked glycans, improving functional predictions. To enhance IgG functionality, producing homogeneous glycoforms is a key step. This review discusses glycan remodeling technologies and their applications in optimizing IgG function.
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Registered trials
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