Thermal unfolding of antibodies
contributed by Nano Temper |
Comparison of nanoDSF and µDSC for thermal stability assessment during biopharmaceutical formulation development
Abstract
Assessing the thermal stability parameters of biologics is an integral part of formulation development in biopharmaceutical research. We compared two methods that detect thermal unfolding transition temperatures (Tm) of a therapeutic monoclonal antibody (mAb): nanoDSF, an advanced differential scanning fluorimetry method, 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. While both nanoDSF and µDSC provided precise and consistent data, the high-throughput and low sample consumption qualify nanoDSF as the ideal technology for thermal stability screening in biopharmaceutical development.
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