Current practices in the biopharmaceutical industry demand rapid process development of multiple therapeutic proteins.  With molecules exhibiting very different physical and chemical characteristics, the platform approaches for downstream processes are often insufficient.  Furthered by material limitations and concurrent upstream process development, this demand can be met through novel experimental design and innovative, bilateral approaches to protein purification.  The traditional scope of purification through chromatography has involved isolating the therapeutic of interest.  Expanding this perspective to better understand the chromatographic behavior of impurities, for example host-cell proteins (HCP), demonstrates a potentially effective tool for developing robust, efficient purification processes.  Utilizing an untransfected parental CHO cell line, 'mock' cultures (containing only HCP) undergo chromatographic separation under conditions similar to their product-containing culture.  Differences in retention behavior can then be exploited in order to ascertain substantial improvements in process performance and impurity removal.

Evaluating the chromatographic behavior of HCP: A tool for rap id process development

245th National Meeting (2013)

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