The assessment of thermal stability parameters of biologics is an integral part of formulation development in biopharmaceutical research. The ever growing number of biologics in the development pipelines worldwide demands rapid and precise methods to quickly screen large sets of conditions in an easy and straight-forward manner.
In our study, we compare two methods for the detection of thermal unfolding transition temperatures (Tm) of a therapeutic monoclonal antibody (mAb): 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. nanoDSF and µDSC both provide precise and consistent data. nanoDSF in addition overcomes 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.