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Novel thermodynamic assay for biomolecular structure stability

7 May 2026

This application note demonstrates a thermodynamic approach to assessing biomolecular structure stability using nano differential scanning calorimetry. The method shows how subtle changes in formulation conditions, such as pH and excipient concentration, can significantly influence protein stability, with high sensitivity and reproducibility. Using the Nano DSC system, the study highlights how thermodynamic profiling enables precise detection of structural changes without the need for sample labeling or modification, supporting more informed decisions in drug development, formulation optimization, and storage stability monitoring.

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CalorimetryCalorimetry is a technique used to determine the heat released or absorbed in a chemical reaction. Calorimeters can be categorized into bomb calorimeters, constant pressure calorimeters, differential scanning calorimeters, isothermal titration calorimeters, X-ray microcalorimeters, heat-loss calorimeters, and high-energy particle calorimeters. The choice of calorimeter depends on the application.Protein StabilityDrug FormulationBiopharmaceuticalsBiopharmaceuticals are proteins and other compounds (such as nucleic acids) produced by living organisms that have uses as therapeutics or for in vivo diagnostics. The most well known example of a biopharmaceutical product, and the first to be approved for therapeutic use, was recombinant human insulin.
Thermodynamic nano DSC assay for biomolecular stability - SelectScience resources