Biopharmaceuticals such as monoclonal antibodies and Fc-fusion proteins have become critically important in the treatment of a range of life-threatening diseases from cancer, and auto-immune diseases to neurodegenerative conditions. However, the development of an effective biopharmaceutical is a complex task that comes with its own challenges. The stability of the therapeutic protein is a remarkable concern that is often governed by several chemical and structural degradation pathways. These pathways may lead to disruption of advanced molecular arrangements i.e. higher-order structure of proteins. This can further lead to the formation of aggregates and/or fragments that can not only reduce efficacy but also elicits undesirable immune responses in patients. Protein aggregates are self-associated protein species that are typically characterized based on five characteristics: size, conformation, chemical modification, reversibility/dissociation, and morphology. Maintenance of accurate higher-order structure is thus, critical to confirm the appropriate functionality, activity, and stability of biopharmaceuticals. An array of systematic analytical methods for the characterization of higher-order-structure is an indispensable element of a complete product characterization program. Various biophysical techniques such as dynamic light scattering (#DLS), size exclusion chromatography (#SEC), analytical ultracentrifugation (#AUC), and size exclusion chromatography with multiple angle light scattering (#SEC-MALS) are thus, used during various stages of product development to get deeper insights about aggregation propensity, unfolding temperature, sedimentation velocity of molecules, distribution of size variants, etc.
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Article by: Amita Puranik (Research Scholar, Institute of Chemical Technology)
