The purification of new recombinant proteins and biopharmaceutical candidates presents a number of challenges in process development. These challenges have led to the emergence of two worlds in protein purification. In the world of high-throughput laboratory screening, affinity tags are universally used to accelerate research and characterization of new products. In the clinical world, tags are forbidden, and new multi-column processes must be used that can take months to develop. Our work provides a platform to bridge these worlds through a practical self-cleaving affinity tag, which enables high-throughput work at laboratory scale while also providing material suitable for clinical studies. In practice, tag self-cleavage is induced by a simple shift in pH, thus releasing it from a resin with a cost, binding capacity and reusability that are attractive for large-scale manufacturing. Most importantly, we have identified factors that influence the cleaving rate and can therefore provide reliable performance over a wide variety of target proteins. This technology is being commercialized by Protein Capture Science. This talk will describe the system and its use, as well as several case studies for proteins produced in HEK, CHO and <i>E. coli</i>, including Covid spike RBD glycoprotein.

Bridging small and large scale manufacturing of non-mAb proteins via a single purification platform

ACS Fall 2021

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