Comparison of nanoDSF and µDSC for Thermal Stability Assessment during Biopharmaceutical Formulation Development

In this study, two methods for the detection of thermal unfolding transition temperatures of a therapeutic monoclonal antibody are compared: nanoDSF, which analyzes changes in the fluorescence emission properties of proteins, and differential scanning calorimetry (µDSC), which detects changes in the heat capacity of a protein solution upon unfolding. The assessment of thermal stability parameters of biologics is an integral part of formulation development in biopharmaceutical research, which demands rapid and precise methods to quickly screen large sets of conditions in an easy and straightforward manner. Both nanoDSF and µDSC provided precise and consistent data. However, nanoDSF overcame several limitations by µDSC, such as low throughput and high sample consumption, and thus represents the ideal technology for rapid and precise thermal stability screening in biopharmaceutical development.