Quantitative assessment of mAb Fc glycosylation of CQA importance by capillary electrophoresis

Marton Szigeti, Jeff Chapman, Beata Borza, Andras Guttman

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The attached carbohydrates at the highly conserved asparagine-linked glycosylation site in the CH2 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.

Original languageEnglish
JournalElectrophoresis
DOIs
Publication statusAccepted/In press - Jan 1 2018

Fingerprint

Glycosylation
Capillary electrophoresis
Capillary Electrophoresis
Polysaccharides
Monoclonal Antibodies
Antibody-Dependent Cell Cytotoxicity
Asparagine
Centers for Disease Control and Prevention (U.S.)
Mannose
Oligosaccharides
Half-Life
Anti-Inflammatory Agents
Carbohydrates
Therapeutics
Serum
Adalimumab

Keywords

  • Biotherapeutics
  • Capillary electrophoresis
  • Critical quality attributes
  • Glycosylation
  • Quantification

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry

Cite this

Quantitative assessment of mAb Fc glycosylation of CQA importance by capillary electrophoresis. / Szigeti, Marton; Chapman, Jeff; Borza, Beata; Guttman, Andras.

In: Electrophoresis, 01.01.2018.

Research output: Contribution to journalArticle

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