The ocular discomfort is the leading cause of contact lens wear discontinuation. Although the tear proteins as a lubricant might improve contact lens adaptation, some in vitro studies suggested that the amount of adsorbed proteins could not simply explain the lubricating performance of adsorbed proteins. The purpose of this study was to quantify the structural changes and corresponding ocular lubricating properties of adsorbed protein on a conventional contact lens material, poly (2-hydroxyethyl methacrylate) (pHEMA). The adsorption behaviors of lysozyme on pHEMA were determined by the combined effects of protein–surface and protein–protein interactions. Lysozyme, the most abundant protein in tear, was first adsorbed onto the pHEMA surface under widely varying protein solution concentrations to saturate the surface, with the areal density of the adsorbed protein presenting different protein–protein effects within the layer. These values were correlated with the measured secondary structures, and corresponding friction coefficient of the adsorbed and protein covered lens surface, respectively. The decreased friction coefficient value was an indicator of the lubricated surfaces with improved adaptation. Our results indicate that the protein–protein effects help stabilize the structure of adsorbed lysozyme on pHEMA with the raised friction coefficient measured critical for the innovation of contact lens material designs with improved adaptation.

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Dental ceramic material is one of the widely preferred restorative materials to mimic the natural tooth enamel surface. However, it has continuously been degraded because of low wear resistance during mastication in the oral cavity. The friction involved was reduced by introducing the lubricant saliva protein layers to improve the wear resistance of the dental materials. However, little is understood regarding how the protein–protein interactions (PPI) influence the adsorbed-state structures and lubricating behaviors of saliva proteins on the ceramic material surface. The objective of this study is to quantify the influences of PPI effects on the structural changes and corresponding oral lubrications of adsorbed α-amylase, one of the abundant proteins in the saliva, on the dental ceramic material with glass as a model surface. α-Amylase was first adsorbed to glass surface under varying protein solution concentrations to saturate the surface to vary the PPI effects over a wide range. The areal density of the adsorbed protein was measured as an indicator of the level of PPI effects within the layer, and these values were then correlated with the measurements of the adsorbed protein’s secondary structure and corresponding friction coefficient. The decreased friction coefficient value was an indicator of the lubricated surfaces with higher wear resistance. Our results indicate that PPI effects help stabilize the structure of α-amylase adsorbed on glass, and the correlation observed between the friction coefficient and the conformational state of adsorbed α-amylase was apparent. This study thus provides new molecular-level insights into how PPI influences the structure and lubricating behaviors of adsorbed protein, which is critical for the innovations of dental ceramic material designs with improved wear resistance.

When an orthokeratology (ortho-k) lens contacts the ocular surface, tear film components such as lipids and proteins rapidly adsorb onto the lens, which may increase friction and contribute to discomfort if not properly removed. Polysaccharides have been reported to reduce protein deposition and improve lubrication, prompting the investigation of alginate acid and lambda-carrageenan in modulating the tribological properties of ortho-k lenses. An in vitro tribological property analysis of ortho-k lenses and protein adsorption and desorption analyses were carried out to investigate the lubricating ability of alginate acid and carrageenan. Zeta potential and turbidity analyses were further conducted to examine potential interactions between polysaccharides and tear film proteins. Tear film proteins significantly increased the friction coefficient of the ortho-k lens, whereas the addition of alginate acid and carrageenan markedly reduced friction. Electrostatic interaction and polysaccharide–protein complex formation were identified as possible mechanisms underlying these effects. These results demonstrate that alginate acid and carrageenan can modify the tribological and interfacial behavior of ortho-k lenses in protein-rich environments, suggesting their potential application in reducing friction-related complications in ortho-k lens wearers.