During the purification of monoclonal antibodies, in a typical process an initial protein A affinity chromatography capture step is followed by one or more intermediate purification or polishing steps to remove any impurities co-eluting with the mAb during the protein A step. These impurities may include protein aggregates. Literature reports have demonstrated as a proof-of-concept the removal of aggregates from a high-titer antibody process by flow-through chromatography with the HIC resin TOYOPEARL Hexyl-650C (S.Ghose, mAbs 5:5, 795–800). Also, our previous research has shown that hydroxyapatite chromatography with CaPure-HA media in bind-and-elute mode provides effective aggregate removal at high-salt and low-phosphate elution conditions, however, step yield is sub-optimal at these conditions (Tosoh Bioscience Application Note 72). These and other preliminary data suggest that hydroxyapatite may be suitable for aggregate removal in flow-through mode. Flow-through mode for aggregate removal provides advantages over bind-and-elute chromatography, including an increase in load ratio and ease of integration into continuous processes. In this study we evaluate the pH, ionic strength, and load mass dependence of flow-through hydrophobic interaction and hydroxyapatite chromatography steps for the removal of aggregates for monoclonal atntibody TBL-mAb-01.

Evaluation of flow-through hydrophobic interaction and hydroxyapatite chromatography steps for the removal of aggregates in the purification of monoclonal antibody TBL-mAb-01

251st National Meeting (2016)

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