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Thermal unfolding of antibodies

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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