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Updated: Jul 7, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
High-pressure differential scanning calorimetry of colorant products
J M Marsh1, C J Clarke, K Meinert
1Procter & Gamble Technical Centers, Rusham Park, Egham Surrey, TW20 9NW, UK.
Abstract:
High-pressure differential scanning calorimetry (HPDSC) can be used to gain information on both the degree of crystallinity in the intermediate filaments (IFs) and the structural rigidity of the surrounding matrix or intermediate filament associated proteins (IFAP) of the hair cortex (1-3). We have used HPDSC to measure changes in the denaturation temperature (T(D)) and enthalpy (DeltaH(D)) of the crystalline components after multiple treatments with permanent hair colorant products. We have observed that after three repeat treatments both the denaturation enthalpy and peak temperature are significantly decreased vs the untreated starting substrate. However, on dialysis of the fibers in deionized water this decrease is shown to be completely reversible, returning the enthalpy and temperature to that of the untreated hair. It is proposed that the decrease is due to the incorporation of formulation components such as the alkalizer and surfactants etc. and metal ions such as calcium and magnesium from the tap wash water. These components are predicted to have a non-permanent effect on the salt bridges and hydrogen bonds and hence the rigidity or viscosity of the matrix. We have compared the denaturation temperature with the tensile properties of the fiber after treatment both before and after removal of actives from the fiber.

