Interaction Between Collagen and Chondroitin-6-Sulfate

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Abstract
The interactions between soluble collagen and chondroitin-6-sulfate in aqueous solution at pH ∼ 4 have been investigated using circular dichroism spectroscopy. This technique has been used to monitor changes in the 'melting' temperature for the collagen triple helix with increasing mucopolysaccharide concentration. The melting point for calf skin collagen, which is normally 38°C, is increased to 46°C in the presence of chondroitin-6-sulfate at a concentration ratio in excess of 5.5 disaccharide residues per 100 amino acids. Thus an interaction occurs between the collagen and mucopolysaccharide, which increases the stability of the former. At concentration ratios below 5.5 disaccharides per 100 amino acids, biphasic melting curves are obtained with transitions at 46°C and 38°C, indicating the presence of both complexed and uncomplexed collagen, which implies that the interaction between the two species is a cooperative phenomenon. These results, along with the known dimensions of the interacting components, suggest that aggregates are formed in solution, consisting of a number of collagen and mucopolysaccharide molecules.