A differential scanning calorimetry analysis of the age-related changes in the thermal stability of rat skin collagen.

Differential scanning calorimetry (DSC) has been applied to the study of connective tissue to evaluate the denaturation process of collagen. We have applied this technique to the study of the ageing of rat skin. We have tried to correlate the variations of the parameters measured by DSC and the modifications of collagen crosslinks with ageing.

Study of the thermal stability of skin collagen by differential calorimetry. Influence of a cosmetic treatment.

Synopsis Collagen being the main structural protein of the skin, the influence of a face cream containing this molecule was studied in the dermis using differential scanning calorimetry. This method, using samples of rat dermis, gives curves from which the denaturation temperature and enthalpy change of the collagen fibre network can be followed. The present study was made using two groups of rats which were treated by the cream (or placebo) during 4 months (5 days a week), and were aged 5 and 9 months at.

Influence of collagen denaturation on the chemorheological properties of skin, assessed by differential scanning calorimetry and hydrothermal isometric tension measurement.

The curves obtained for skin samples of different ages and species by hydrothermal isometric tension ("HIT") measurement are compared to those obtained by differential scanning calorimetry (DSC) under the same thermal conditions (for a rise in temperature at a rate of 1.0 degrees C/min). Collagen denaturation, observed by DSC, directly affects the kinetics of the tension variations in the first part of the "HIT" curves, including the early peak due to the presence and destruction of the heat-labile cross-links in the collagen network.