DSC: The Universal Macromolecular Stability Monitor
Differential scanning calorimetry is a universal bioassay system for measuring the stability of biological macromolecules. In a DSC experiment a biomolecule is typically heated at 0.1 to 5oC/min and the heat (DH) and the temperature (TM) of denaturation is monitored. It shares many properties with isothermal titration calorimetry including its ability to detect very small changes in temperature and the related advantages of no ‘tagging’ requirements and little or no assay development. TM shifts are a readily accessible probe for the stability of biomolecules and have wide applications in the drug discovery and development arenas. Small molecule interactions with protein or nucleic acid targets induce TM shifts, a phenomenon that is readily exploited to screen for drug candidates. In addition the stability of protein biopharmaceuticals can be determined and used to find stable protein constructs and excipients to increase shelf lives
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