Structural influence of mono and polyhydric alcohols on the stabilization of collagen.

In the present study, solvents effects on the structure of collagen have been examined by circular dichroism and their interfacial tension at glass/liquid and Teflon/liquid. Changes in the conformations of the protein have been analyzed after equilibration with aqueous solutions of monohydric and polyhydric alcohols like methanol, ethanol, n-propanol, propane-2-diol and glycerol. The results from viscosity and Circular dichroism (CD) spectra suggest a clear distinction in the structural changes for collagen with monohydric alcohols as against polyhydric ones. The surface tension and interfacial tension at glass (high surface energy, HFSE) and Teflon (Low surface energy, LSFE) reflect similar differences between the monohydric and polyhydric alcohols. Studies on the interfacial energy of the adsorbed protein at glass/solution interface compared to that of Teflon/solution interface show that the water structure near glass gets perturbed leading to an increase in the average free energy of the bulk water phase and a reduction in hydrophobic effect near the glass. The results suggest that the different solvents alter the hydrophobic effect on the hydrated protein to different extent and thus influence folding equilibrium of the protein without directly interacting with it. Polyhydric alcohols seem to favor the native collagen structure while monohydric alcohols enhance it.