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The stability of a candidate drug-protein is critical to the success or failure of its development as a viable drug. Low stability could adversely impact production consistency, shipping and handling excursions, and long-term storage. Developability assessments are becoming an increasingly important criterion to mitigate this risk. The conventional approach is to perform the developability assessment on the final few shortlisted candidates at the mid-to-late stage of drug development.

At Aragen, we have moved the developability assessment into the discovery phase during antibody screening, accelerating the candidate selection process. Integration of the Uncle platform into our process was essential for early assessments due to its small sample requirements and rapid analysis time. In this study, we show that humanized antibody candidates of a murine monoclonal antibody differ in their thermal melting and thermal aggregation profiles due to differences in the stability of the Fab domain (that carries the target binding residues) because of the humanization process. Destabilization of the Fab domain or lower aggregation onset can lead to problems later during production, shipment, or storage. Assessment of thermal stability and aggregation potential can be an important tool for early selection of viable drug candidates. Analysis during antibody screening (discovery stage) and clone selection (early process development stage) can significantly reduce the time and cost of downstream manufacturing.

Produced with support from:

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Jackie Kennedy-Wilde,
Aragen Bioscience

Dina Finan, Ph.D.
Product Manager,
Unchained Labs