Unraveling the Twin Tales of Biosimilar and Innovator Glycans

N-Glycan Characterization and the Future of Method Standardization

N-glycans are omnipresent in the Fc region of monoclonal antibody products. Modifications to a glycan profile can impact a protein’s stability/folding, binding affinities, effector functions, clearance rates, and/or immunogenicity. Their characterization is critical to ensuring efficacy and safety in patients. The multitude of glycan characterization methods, each with different levels of sensitivity and reliability, complicates standardization efforts. To tackle this, we’ve conducted comparative glycan analysis studies, examining various innovator mAbs, their biosimilars, and different characterization techniques for NIST mAb.

Key take aways:

• Comparison of innovator anti-TNF⍺ mAbs (Humira^®, Remicade^®, Simponi Aria^®) and trastuzumab biosimilars (Kanjinti^®, Ogivri^®) with reference drugs.
• Highlighting the impact of glycan differences in mAbs on patient experience.
• Suggesting future standardization approaches for glycan characterization in mAbs.

Jill Kinzer is a scientist at MS Bioworks, a contract proteomics research company based in Ann Arbor, Michigan. During her Ph.D. (Pharmaceutical Sciences, Uni Michigan, under Dr Anna Scwendeman), Jill introduced automation into MS Bioworks’ post translational modification identification and quantitation workflows. Jill has authored six papers on monoclonal antibody characterization methods and is looking forward to publishing more on her current work streamlining plate-based proteomics assays.