Effects of sialic acid linkage on antibody-fragment crystallizable receptor binding and antibody dependent cytotoxicity depend on levels of fucosylation/bisecting

Fragment crystallizable (Fc) glycosylation of immunoglobulin G-type monoclonal antibodies applied to therapeutic applications is regarded a critical quality attribute and can influence bioactivity, pharmacokinetics and/or immunogenicity/safety. Investigating the impact of certain Fc N-glycans is th...

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Veröffentlicht in:	Bioanalysis 2019-08, Vol.11 (15), p.1437-1449
Hauptverfasser:	Thomann, Marco, Malik, Sebastian, Kuhne, Felix, Avenal, Cecile, Plath, Friederike, Bonnington, Lea, Reusch, Dietmar, Bulau, Patrick, Cymer, Florian
Format:	Artikel
Sprache:	eng
Schlagworte:	ADCC Antibodies antibody Antibody-Dependent Cell Cytotoxicity Biological activity Chromatography Cytotoxicity effector functions Fucose - metabolism fucosylation Galactose glycoengineering Glycosylation Humans Immunogenicity Immunoglobulin G Immunoglobulin G - metabolism Mass spectrometry Monoclonal antibodies N-Acetylneuraminic Acid - metabolism N-glycans Neuraminic Acids - chemistry Neuraminic Acids - metabolism Peptides Pharmacokinetics Phosphatase Polysaccharides Protein Binding Proteins Receptors, IgG - metabolism Scientific imaging sialylation Standard deviation Therapeutic applications
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