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Updated: May 16, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Quantitative description of temperature induced self-aggregation thermograms determined by differential scanning
Leonardo Chiappisi1, Giuseppe Lazzara, Michael Gradzielski
1Stranski-Laboratorium für Physikalische Chemie und Theoretische Chemie, Institut für Chemie, Technische Universität Berlin, Sekr. TC 7, Strasse des 17. Juni 124, D-10623 Berlin, Germany. leonardo.chiappisi@tu-berlin.de
Abstract:
A novel thermodynamic approach for the description of differential scanning calorimetry (DSC) experiments on self-aggregating systems is derived and presented. The method is based on a mass action model where temperature dependence of aggregation numbers is considered. The validity of the model was confirmed by describing the aggregation behavior of poly(ethylene oxide)-poly(propylene oxide) block copolymers, which are well-known to exhibit a strong temperature dependence. The quantitative description of the thermograms could be performed without any discrepancy between calorimetric and van 't Hoff enthalpies, and moreover, the aggregation numbers obtained from the best fit of the DSC experiments are in good agreement with those obtained by light scattering experiments corroborating the assumptions done in the derivation of the new model.
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