Glycan Analysis

The biological activity, stability, biological half-life, and immunogenicity of biological drugs can all be significantly impacted by protein glycosylation. One type of post-translational modification is glycosylation. It is an enzymatic modification process that is not template-driven, in contrast to transcription. As a result, the conditions of manufacture can affect glycosylation. Understanding the structure-activity link requires an understanding of glycosylation characterisation. For instance, removing core fucose from the N-glycans on the heavy chain of IgG1 can greatly increase FcγRIIIa’s binding affinity, which in turn increases the cytotoxic potential of cells that are dependent on antibodies. The production of many biopharmaceuticals in non-human cell lines may lead to an increase in the glycosylation of non-human types. This could result in altered immunogenicity, which could have therapeutic ramifications like decreased efficacy, altered pharmacokinetics, hypersensitivity and generalized immunological reactions, and medication neutralization.

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