Enamel matrix proteins in promoting saliva lubrication

Abstract

Anti-wear performance of human enamel in the mouth is closely related to the lubrication of salivary pellicle. It is well known that the inorganic hydroxyapatite (HA) of the enamel plays an important role in the adsorption and pellicle-forming of salivary proteins on the enamel, but the role of enamel matrix proteins remains unclear. In this study, the adsorption and lubrication behavior of salivary proteins on original, heated, and deproteinated enamel surfaces was comparatively investigated using an atomic force microscopy and nano-indentation/scratch techniques. Compared with that on the original enamel surface, the adsorption and lubrication behavior of salivary proteins remains almost unchanged on the heated enamel surface (where the enamel matrix proteins are denatured but the size of HA crystalline nanoparticles keeps constant) but exhibits an obvious compromise on the deproteinated enamel surface (where the enamel matrix proteins are removed and agglomeration of HA crystallites occurs). The HA agglomeration weakens the electrostatic interaction of enamel surfaces with salivary proteins to cause a distinct negative influence on the adsorption and pellicle-forming of salivary proteins. Further, the negative effect is confirmed with a quartz crystal microbalance with dissipation. In summary, by regulating enamel nanostructure for appropriate electrostatic interactions between salivary proteins and enamel surfaces, the enamel matrix proteins play an essential role in the adsorption and pellicle-forming of salivary proteins on human enamel, and then contribute to saliva lubrication, which provides the enamel with an anti-wear mechanism. The findings will promote and assist the design of enamel-inspired anti-wear materials.