Application Notes

Comparison of nanoDSF and µDSC for thermal stability assessment during biopharmaceutical formulation development

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APPLICATION NOTE Thermal Unfolding of Antibodies Comparison of nanoDSF and µDSC for thermal stability assessment during biopharmaceutical formulation development Dennis Breitsprecher 1 , Nils Glücklich 2 , Andrea Hawe 2 , Tim Menzen 2 1 NanoTemper Technologies GmbH, Munich, Germany 2 Coriolis Pharma Research GmbH, Munich, Germany Abstract 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 (T m ) of a therapeutic monoclonal antibody (mAb): nanoDSF, which analyzes changes in the fl uorescence emission properties of proteins, and diff erential 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. Introduction The thermal stability of a protein is routinely used as one main indicator for its physical stability which aff ects long-term storage in a given formulation. Historically, µDSC has been used during formulation development. This approach measures

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