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Use of Differential Scanning Calorimetry (DSC) in biopharmaceutical development
Differential scanning calorimetry (DSC) is an established biophysical tool for protein stability characterization during biopharmaceutical drug development. DSC data are used to advance the most stable and 'developable' proteins into the pipeline, and optimize the process and formulation conditions to maintain protein stability during manufacturing and storage.
DSC determines the thermal transition midpoint (TM). For a protein which reversibly denatures, TM is the temperature where 50% of the protein is in its native (folded) conformation, and 50% is in its denatured (unfolded) conformation. TM is considered a good indication of thermal stability – the higher the TM, the more thermally stable the protein. Even if a protein is irreversibly denatured during DSC, the TM provides important insights into its thermal stability. Multi-domain proteins, like antibodies, typically have more than one unfolding domain, and DSC detects multiple TMs. In a recent survey of biopharmaceutical scientists, DSC was rated as a 'very useful' to 'extremely useful' biophysical tool for candidate selection, formulation development, product characterization, comparability, and biosimilarity.
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