Glycosylation

Glycosylation is considered the most important post-translational modification (PTM) in biopharmaceuticals. More than half of all human proteins are glycosylated, regulating both their structure, function and half-life. Different types of glycosylation exist, the best known being N- and O-linked glycosylation present on asparagin and serine or threonine residues, respectively.

Glycostructures not found naturally in humans have the potential to be immunogenic. In the past years, the elucidation of carbohydrate structures on therapeutically active proteins has become of great importance. It is fostered by the development and advancement of highly elaborate analytical techniques such as mass spectrometry, nuclear magnetic resonance, hplc and capillary electrophoresis.

Further characterization of carbohydrates is achieved by e.g., enzymatic digestion, specific staining, lectin binding or isoelectric focusing methods.
The most important monosaccarides appearing in mammalian carbohydrate structures are D-glucose, D-galactose, D-mannose, N-acetyl-D-glucosamine, L-fucose and N-acetyl neuraminic acid. These sugars build up the diverse branched structures possible on a human protein also normally resulting in considerable microheterogenity.

CEVEC’s Amniocyte Production (CAP) Technology based on human amniocytes offers protein production at its best:

• Produce original human glycosylation for complex proteins
• Include authentic sialylation for improved half-live
• Avoid immunogenic non-human carbohydrate residues