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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.

SUBMITTER: Baskaran N

PROVIDER: S-EPMC7463787 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:For further the understanding of the adsorption mechanism of heavy metal ions on the surface of protein-inorganic hybrid nanoflowers, a novel protein-derived hybrid nanoflower was prepared to investigate the adsorption behavior and reveal the function of organic and inorganic parts on the surface of nanoflowers in the adsorption process in this study. Silk fibroin (SF)-derived and copper-based protein-inorganic hybrid nanoflowers of SF@Cu-NFs were prepared through self-assembly. The product was characterized and applied to adsorption of heavy metal ion of Pb(II). With Chinese peony flower-like morphology, the prepared SF@Cu-NFs showed ordered three-dimensional structure and exhibited excellent efficiency for Pb(II) removal. On one hand, the adsorption performance of SF@Cu-HNFs for Pb(II) removal was evaluated through systematical thermodynamic and adsorption kinetics investigation. The good fittings of Langmuir and pseudo-second-order models indicated the monolayer adsorption and high capacity of about 2000 mg g-1 of Pb(II) on SF@Cu-NFs. Meanwhile, the negative values of ? r G m ( T ) ? and ? r H m ? proved the spontaneous and exothermic process of Pb(II) adsorption. On the other hand, the adsorption mechanism of SF@Cu-HNFs for Pb(II) removal was revealed with respect to its individual organic and inorganic component. Organic SF protein was designated as responsible 'stamen' adsorption site for fast adsorption of Pb(II), which was originated from multiple coordinative interaction by numerous amide groups; inorganic Cu3(PO4)2 crystal was designated as responsible 'petal' adsorption site for slow adsorption of Pb(II), which was restricted from weak coordinative interaction by strong ion bond of Cu(II). With only about 10% weight content, SF protein was proven to play a key factor for SF@Cu-HNFs formation and have a significant effect on Pb(II) treatment. By fabricating SF@Cu-HNFs hybrid nanoflowers derived from SF protein, this work not only successfully provides insights on its adsorption performance and interaction mechanism for Pb(II) removal, but also provides a new idea for the preparation of adsorption materials for heavy metal ions in environmental sewage in the future.

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

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