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Introduction to HILIC for Biopharmaceuticals

The importance of the glycosylation / glycoprofiles for protein biopharmaceuticals has already been discussed in relation to its lot-to-lot variability and biosimilar and biobetter development.  However, it is worth revisiting briefly as it useful putting these facets in context of the liberation, clean-up, labelling, separation, and finally detection of glycans.

Glycosylation is a Critical Quality Attribute (CQA) as increased efficacy by way of increased antibody-dependent cell-mediated cytotoxicity (ADCC) through afucosylation.  In addition, certain glycotropes and / or specific glycans such as N-glycolneuraminic acid can lead to an increase in immunogenicity.  Finally, a reduction in half-life can be observed due to the presence of high mannose glycans, with their associated clearance rates being elevated. 

When looking to control glycoprofiles a key variable is the cell culture used for recombinant expression – in particular the choice of the mammalian host, the cell culture process conditions (such as temperature and duration), and input materials (such as type and quantity of activators and substrates) to name but a few.

Approximately 40% of all protein biopharmaceuticals are glycoproteins with a glycan mass range of 2 – 3% for monoclonal antibodies (mAbs) and up to 50% for erythropoietin (EPO).  Figure 1 shows free or unglycosylated EPO and Figure 2 shows modern EPO in its glycosylation state.

Figure 1:
Unglycosylated EPO
Unglycosylated EPO

Figure 2:
Glycosylated EPO

Unglycosylated EPO
 
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