N-glycosylation heterogeneity and the influence on structure, function and pharmacokinetics of monoclonal antibodies and Fc fusion proteins

[Display omitted] Monoclonal antibody and Fc fusion protein drugs are complex heterogeneous mixtures of numerous different protein variants and modifications. N-glycosylation as one of the most complex post-translational modification influences the structural characteristics of the antibodies Fc par...

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Veröffentlicht in:European journal of pharmaceutics and biopharmaceutics 2016-03, Vol.100, p.94-100
Hauptverfasser: Higel, Fabian, Seidl, Andreas, Sörgel, Fritz, Friess, Wolfgang
Format: Artikel
Sprache:eng
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Zusammenfassung:[Display omitted] Monoclonal antibody and Fc fusion protein drugs are complex heterogeneous mixtures of numerous different protein variants and modifications. N-glycosylation as one of the most complex post-translational modification influences the structural characteristics of the antibodies Fc part thereby potentially modulating effector function and pharmacokinetics. Several investigations on the relationship between N-glycosylation and pharmacokinetics have been published. However, this structure–function relationship is not fully understood. In this review potential alterations with focus on N-glycosylation of mAbs and Fc fusion proteins and the possible effects on the pharmacokinetics are reviewed and the current understandings of the underlying mechanisms are described.
ISSN:0939-6411
1873-3441
DOI:10.1016/j.ejpb.2016.01.005