One of the inherent bottlenecks in screening discovery-phase biologics is the lack of a simple standardized downstream purification platform. While Protein A has been transformative in high-throughput screening of mAb variants, there is no analogous platform technology for downstream processing of non- mAb protein therapeutics. Screening throughput will always be limited when reliant on complex networks of traditional multi-column chromatographic processes, since these must be tailored specifically to each product. The common solution at lab scale is to add affinity tags, but this often alters the native form or function of the protein.<br/>To resolve these issues, our work focused on development of a novel affinity capture-based technique mediated by an engineered split-intein. This approach allows potentially any recombinant protein to be selectively immobilized, and subsequently released as a tagless, traceless product. The work presented will focus on development of the platform, demonstration of characterization activities in a HTS 96-well filter-plate format, optimizing performance on mini-columns using TECAN-automated robotic chromatography, and prospective applications to accelerate high-throughput purification of discovery-phase recombinant proteins.<br/>

Intein-mediated affinity capture: A novel platform enabling rapid prototyping and characterization of discovery-phase biologics by single-column purification and integrated tag removal

2019 Spring National Meeting

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