Protein aggregation is a growing problem in the manufacturing of biologics due to increasing solution titers. Antibody aggregates often are removed in a three/four-step process involving a bind-and-elute cation-exchange chromatography step and additional hydrophobic interaction chromatography (HIC) columns after an initial Protein A capture step. We are presenting case studies in which aggregates and host cell proteins (HCP) are removed in a two-step monoclonal antibody (mAb) purification scheme. In this scheme, the mAb is isolated from supernatant using a Protein A chromatography step followed by a polishing step purification using Purilogics’ multimodal anion-exchange membrane chromatography columns (MMM-AEX) operating in flow-through mode.<br/><br/>In this study, a variety of mAbs were purified using the two-step purification strategy. Different buffer types (e.g. tris base, phosphate buffers) and buffer conductivities (1-15 mS/cm) were explored. HCP level and fractions of monomer, dimer and aggregates were compared before and after the polishing step. The results were compared with studies using two other leading commercial membrane products. In addition to reporting these data, we will demonstrate the MMM-AEX column scalability and reusability.

Application of novel multimodal anion-exchange membrane chromatography columns in a two-step mAb purification scheme: Aggregates and HCP removal

2019 Spring National Meeting

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