Glycosylation of monoclonal antibodies is one of the common post translation modifications. These glycoprotein biopharmaceuticals contain complex oligosaccharide moieties whose presence, absence, sites of attachment, and relative abundance profiles can have significant impact on the efficacy, pharmacokinetics, immunogenicity, folding, and stability of a drug.
The glycan moieties have a key role in immunogenicity, effector function efficacy, and clearance of the mAbs. The stability of a recombinant protein therapeutic requires long term monitoring throughout the shelflife of the product for important modifications, such as glycosylation. glycosylation can be analyzed on the intact protein, but glycopeptide mapping is necessary to provide additional critical information such as sequence information, mass analyses, and identification of the glycosylation sites.
Shimadzu offers accurate solutions for characterizing glycan structure and monitoring glycan profiles using MALDI-MS technology, LC/MS and liquid chromatography systems.