Quantify the Protein–Protein Interaction Effects on Adsorption Related Lubricating Behaviors of α-Amylase on a Glass Surface

Abstract

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.

Correction: Wei, Y.; et al. Quantify the Protein-Protein Interaction Effects on Adsorption Related Lubricating Behaviors of α-Amylase on a Glass Surface. Polymers 2020, 12, 1658

“…The authors wish to make the following corrections to this paper [ 1 ]: in the original version of our article, some of the data in Figures 1, 2, 3, and 5 were collected mistakenly from Lysozyme (Sigma, St. Louis, MO, USA), rather than α-amylase (EC 3.2.1.1) from barley malt (HIMEDIA, West Chester, PA, USA). We apologize for the original error.…”