Interaction of Hyaluronan Acid with Some Proteins in Aqueous Solution as Studied by NMR

According to actual literature data, hyaluronic acid (HA) that is presented in the extracellular matrix can interact with proteins and thereby affect several important functions of the cell membrane. The purpose of this work was to reveal the features of the interaction of HA with proteins using the PFG NMR method by sampling two systems: aqueous solutions of HA with bovine serum albumin (BSA) and aqueous solutions of HA with hen egg-white lysozyme (HEWL). It was found that the presence of BSA in the HA aqueous solution initiates a certain additional mechanism; as a result, the population of HA molecules in the gel structure increases to almost 100%. At the same time, for an aqueous solution of HA/HEWL, even in the range of low (0.01–0.2%) HEWL contents, strong signs of degradation (depolymerization) of some HA macromolecules were observed such that they lost the ability to form a gel. Moreover, lysozyme molecules form a strong complex with degraded HA molecules and lose their enzymatic function. Thus, the presence of HA molecules in the intercellular matrix, as well as in the state associated with the surface of the cell membrane, can, in addition to the known ones, perform one more important function: the function of protecting the cell membrane from the destructive action of lysozymes. The obtained results are important for understanding the mechanism and features of the interaction of extracellular matrix glycosaminoglycan with cell membrane proteins.