Eight Reasons to Use MicroCal PEAQ-DSC Automated System

The new MicroCal PEAQ-DSC Automated system

Eight reasons to upgrade from the MicroCal VP-Capillary DSC system

Use of Differential Scanning Calorimetry (DSC) in biopharmaceutical development

Differential scanning calorimetry (DSC) is an established biophysical tool for protein stability characterization during biopharmaceutical drug development. DSC data are used to advance the most stable and 'developable' proteins into the pipeline, and optimize the process and formulation conditions to maintain protein stability during manufacturing and storage.

DSC determines the thermal transition midpoint (T_M). For a protein which reversibly denatures, T_M is the temperature where 50% of the protein is in its native (folded) conformation, and 50% is in its denatured (unfolded) conformation. T_M is considered a good indication of thermal stability – the higher the T_M, the more thermally stable the protein. Even if a protein is irreversibly denatured during DSC, the T_M provides important insights into its thermal stability. Multi-domain proteins, like antibodies, typically have more than one unfolding domain, and DSC detects multiple T_Ms. In a recent survey of biopharmaceutical scientists, DSC was rated as a 'very useful' to 'extremely useful' biophysical tool for candidate selection, formulation development, product characterization, comparability, and biosimilarity^[1].