Abstract
Adsorption behavior and stabilization/ destabilization effects of 2-hydroxyethyl methacrylate (HEMA) on a bovine tendon collagen (BTC) (type I) , either native (N) or thermally denatured (D) , were studied by IR spectroscopy and differential scanning calorimetry (DSC) . The amount of HEMA adsorbed was larger on BTC (D) than on BTC (N) , because BTC (D) had a larger specific surface area (SSA) as revealed from SSA measurement. Denaturation temperature (Td) of BTC (N) , measured by DSC in aqueous HEMA solution, decreased from 63°C to 40°C with increasing HEMA concentration (CHEMA) up to 20 wt%. This destabilization might be caused by the loss of hydrophobic stabilization of the helix structure as CHEMA was increased. At CHEMA>20 wt%, the structure of collagen was restabilized presumably due to the dehydration effect conferred by HEMA at higher concentration. BTC (D) with little helix content, however, showed only a weak endothermic peak in the DSC measurement and the Td at 40°C was independent of CHEMA.
