Dielectric relaxation studies of collagen - surfactant complexes in aqueous buffer solution.

Dielectric relaxation studies of rat tail tendon collagen with anionic sodium dodecyl sulphate (SDS), cationic cetyltrimethyl ammonium bromide (CTAB) and nonionic Tween 80 in aqueous buffer solutions at four different temperatures have been carried out in the frequency range 1 GHz to 25 GHz using time domain dielectric spectroscopy. The frequency dependent normalized dielectric modulus function P of the collagen and surfactant solutions show up as peaks around 1-2 GHz which is due to the bound water around collagen macromolecule and surfactant micelles. For the collagen - surfactant complexes, the peak in normalized dielectric modulus function P is shifted towards high frequency side near 2-3 GHz upon addition of surfactants to collagen in buffer solution. The water structure around collagen is altered in the presence of micelle forming surfactant additives and this change may affect the degrees of freedom of their motion. Hence the significant changes are observed in the relaxation time of bound water around collagen macromolecule in the presence of surfactants. Further, it was observed that no considerable change in relaxation time of hydration water of the complexes with respect to change in temperature within the studied temperature range. The activation enthalpy and activation entropy for the dipolar orientation corresponding to the free water for the surfactants and their complexes with collagen have been calculated from the Arrhenius plot. Our thermodynamic results suggest that the two‑hydrogen-bonded model may be possible in SDS and Tween 80 environments, whereas the one‑hydrogen-bonded model is likely to be possible in buffer and CTAB environments.