Mike May PhD
A protein’s activity arises from its structure. In bioprocessing, a protein’s secondary structure—twists like an alpha-helix or folds like a beta-pleated sheet—plays a fundamental role in the performance of a biotherapeutic. “Very small changes in the structure of a protein and peptide biotherapeutic could affect its accuracy and specificity,” says Jeff Zonderman, chief commercial officer at RedShift BioAnalytics in Burlington, MA.
Processing a protein can change its secondary structure. The denaturing of proteins in frying an egg, for example, resembles aggregation that can arise in bioprocessing. This clumping in a biotherapeutic not only impacts its efficacy, but can turn it toxic. That explains the industry’s interest in this process, which was described in “Aggregation Analysis.”