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Quantitative assessment of mAb Fc glycosylation of CQA importance by capillary electrophoresis
Author(s) -
Szigeti Marton,
Chapman Jeff,
Borza Beata,
Guttman Andras
Publication year - 2018
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201800076
Subject(s) - glycosylation , glycan , monoclonal antibody , chemistry , antibody dependent cell mediated cytotoxicity , oligosaccharide , n linked glycosylation , asparagine , capillary electrophoresis , biochemistry , monoclonal , antibody , glycoprotein , biology , chromatography , enzyme , immunology
The attached carbohydrates at the highly conserved asparagine‐linked glycosylation site in the C H 2 domain of the fragment crystallizable (Fc) region of monoclonal antibody therapeutics can play an essential role in their mechanism of action, including ADCC, CDC, anti‐inflammatory functions, and serum half‐life. Thus, this particular glycosylation represents one of the important critical quality attributes (CQA) of therapeutic monoclonal antibodies, which should be closely monitored and controlled during all stages of biopharmaceutical manufacturing. To study Fc glycosylation related quantitative critical quality attributes, the N‐glycan pool of adalimumab (Humira ® ) was spiked with increasing amounts of mannose‐5 oligosaccharide, a glycan with high CQA importance. The method enabled precise quantitative CQA assessment with high detection sensitivity.