Interactions between mucopolysaccharides and cationic polypeptides in aqueous solution: Hyaluronic acid, heparitin sulfate, and keratan sulfate

Abstract

Circular dichroism spectroscopy has been used to study the interactions of hyaluronic acid, heparitin sulfate, and keratan sulfate with cationic polypeptides. The results indicate that the presence of these mucopolysaccharides has an effect in the conformation of poly(L‐lysine) and poly(L‐arginine), such that the former adopts the “random” form and the latter takes up the α‐helical conformation, rather than the “charged coil” form expected at neutral pH. The relative strengths of the interactions can be judged from the melting temperatures above which they are disrupted. Both the stoichiometry and the strength of the interactions depend on the position, number, and type of anionic groups attached to the polysaccharide backbone. Such considerations place the six common mucopolysaccharides in order of increasing strength of interaction: hyaluronic acid < chondroitin 4‐sulfate < heparitin sulfate < chondroitin 6‐sulfate < keratan sulfate ⩽ dermatan sulfate. These differences should be paralleled by differences in the interaction of the mucopolysaccharides with collagen and fibrous proteins.