Monoclonal antibodies (mAbs) have emerged as a highly effective class of protein therapeutics for treating various diseases. Their ability to target specific tissues and modulate cellular activities makes them valuable tools in modern medicine. Cellular production and downstream manufacturing processes commonly introduce heterogeneity to the mAb structure by way of post-translational or chemical modifications, including lysine truncation, asparagine deamidation and glycosylation. This can alter the charge of the biomolecule by addition or elimination of cationic or anionic sites, resulting in increased charge heterogeneity that can have potential effects on product efficacy, safety and stability.
Similarly, adeno-associated viruses (AAV) — the main biopharmaceutical gene delivery viral vectors for use in gene therapy treatment of a variety of human diseases — could contain many types of process- and product-related impurities. Full characterization, including quantitation of the empty and full capsids of a given AAV therapeutic, are important for understanding their quality and potential efficacy.
Ion exchange separations are routinely used for quality attribute profiling of various biopharmaceutical formats, be it charge variant analysis of monoclonal antibodies and recombinant proteins, or determining the capsid fill state of viral vectors for gene therapy.
An upcoming webinar titled “A Novel Ion Exchange Phase Media for High-Resolution Charge Profiling of Various Biopharmaceutical Modalities,” on Aug. 9, 2023, will present a novel stationary phase media based on 3 mm monodispersed particles size for ion exchange separations — both cation and anion exchangers — that can deliver the highest resolution separation with lot-to-lot consistency. Dr. Jonathan Bones (principal investigator from NIBRT) and Dr. Ke Ma (staff scientist, Research & Development, Thermo Fischer Scientific) will present application results using this new monodispersed particle column for charge variant profiling of mAbs and their various biosimilars, and the determination of full and empty AAV viral vector chromatographic separation hyphenated with native MS and direct mass technology mode charge detection will be described.
Register for the webinar to learn more and engage with the panelists.