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The interaction between bovine tendon collagen and a series of homologous alcohols were investigated using a differential scanning calorimetry. For all alcoholic substances, as well as 2-hydroxyethyl methacrylate (HEMA), the concentration dependence of the denaturation temperature of collagen was observed, which showed a minimum at 30%. Clearly there are two opposing actions on the stabilization of the collagen structure; destabilization dominates over stabilization at lower concentrations, and vice versa at higher concentrations. The concentration dependence became greater for longer chain alcohols, while it was suppressed by the increased number of OH groups. The chain length-dependent surface tension may be related, which controls the permeation of the additives through the collagen fibers. Overall hydrophobicity, indicated by the hydrophile-lipophile balance (HLB) numbers, suggests the importance of the hydrophobic effect in the interaction of collagen and alcoholic substances, including adhesive monomers such as HEMA.

The Effects of Alcoholic Compounds on the Type I Collagen Studied by Differential Scanning Stability of Calorimetry.