During monoclonal antibody (mAb) purification, high molecular weight species are normally removed using one or more additional chromatography steps, such as a hydrophobic interaction chromatography step. Existing multimodal ion-exchange resin-based chromatography columns combine hydrophobic interactions and columbic forces together. However, they often fail to provide satisfying capacity to remove host cell proteins (HCPs), aggregates and virus particles simultaneously, particularly in a two-chromatography-step purification scheme. Here, we present feasibility studies applying Purilogics’ multimodal anion-exchange membrane chromatography columns (PurexaTM-MQ) to remove HCP and aggregates from mAb streams purified by Protein A chromatography. The data indicates that a very high volume of antibody stream could be loaded onto PurexaTM-MQ columns to obtain purified mAbs with low aggregate and HCP levels. In addition, we conducted virus loading challenges with spiked protein and DNA in various buffer conditions. The results suggest more than a 4 log reduction of virus can be achieved. PurexaTM-MQ columns offer promising results to simplify mAb purification and achieve process compression.

Process intensification feasibility studies using novel multimodal anion-exchange membrane chromatography columns

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.