Influence of hydrogen bond, hydrophobic and electrovalent salt linkages onthe transition temperature, enthalpy and activation energy in rat tail tendon (RTT) collagen fibre

The influence of hydrogen bonding, hydrophobic and electrostatic interactio ns on the thermal stability of rat tail tendon collagen fibre has been stud ied using differential scanning calorimetry (DSC) and hydrothermal isometri c tension (HIT) experiments. The reagents used to study these effects are u rea (hydrogen bonding), aqueous alcohols (hydrophobic) and 0.02 M Tris-male ate buffer at pH 4-8 (electrostatic interactions). The peak temperature, en thalpy changes and energy of activation for collagen to gelatin transition are computed using DSC. The peak temperature and enthalpy changes decrease with increasing concentrations of urea, increasing chain length of alcohol and decreasing pH. The shape of the isometric tension curves of the collage n fibres provide information on the crosslinking of collagen fibre while th e extent of relaxation after maximum tension is indicative of thermally sta ble crosslinks. (C) 1999 Published by Elsevier Science B.V. All rights rese rved.