Directed 2-dimensional organisation of collagen: role of cross-linking and denaturing agents

Abstract

The effect of additives like curcumin and surfactants on the self-assembly of collagen from a simple 2-dimensional system of Langmuir films of the protein at air/solution interface has been attempted in this study using quartz crystal microbalance (QCM) and dynamic surface tensiometer. Though pure curcumin is not surface active, a synergistic effect of collagen with curcumin seems to lead to enhanced surface activity in the protein. In general, the presence of additives, increases the surface activity of collagen even for the lowest concentration and the largest change in surface activity is seen for collagen with sodium dodecyl sulfate (SDS). The results suggest interplay between the unexposed hydrophobic groups, and the opening out and solvation of the more charged or polar groups at the surface leading to aggregation followed by self-assembly. Modulation of aggregation at interface in collagen due to these additives may be an approach that could be explored for possible applications in bio-materials and for delivery of protein-drug complexes.