Development of recombinantly expressed therapeutic proteins as biopharmaceuticals hold the great advantage of biocompatibility and biodegradability. The success of such protein-based drug formulation relies on a deep understanding of the physicochemical stability throughout the production process until the long-term storage.
In this application note, thermal denaturation of bovine serum albumin (BSA) was investigated as important tool to monitor the conformational changes which disrupt the highly ordered structure of the native state of the protein and, in turn, affect its biological activity.