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

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 sali...

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Autores principales: Baskaran, Nareshkumar, Chang, You-Cheng, Chang, Chia-Hua, Hung, Shun-Kai, Kao, Chuan-Tse, Wei, Yang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7463787/
https://www.ncbi.nlm.nih.gov/pubmed/32722491
http://dx.doi.org/10.3390/polym12081658
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author Baskaran, Nareshkumar
Chang, You-Cheng
Chang, Chia-Hua
Hung, Shun-Kai
Kao, Chuan-Tse
Wei, Yang
author_facet Baskaran, Nareshkumar
Chang, You-Cheng
Chang, Chia-Hua
Hung, Shun-Kai
Kao, Chuan-Tse
Wei, Yang
author_sort Baskaran, Nareshkumar
collection PubMed
description 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.
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spelling pubmed-74637872020-09-02 Quantify the Protein–Protein Interaction Effects on Adsorption Related Lubricating Behaviors of α-Amylase on a Glass Surface Baskaran, Nareshkumar Chang, You-Cheng Chang, Chia-Hua Hung, Shun-Kai Kao, Chuan-Tse Wei, Yang Polymers (Basel) Article 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. MDPI 2020-07-25 /pmc/articles/PMC7463787/ /pubmed/32722491 http://dx.doi.org/10.3390/polym12081658 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Baskaran, Nareshkumar
Chang, You-Cheng
Chang, Chia-Hua
Hung, Shun-Kai
Kao, Chuan-Tse
Wei, Yang
Quantify the Protein–Protein Interaction Effects on Adsorption Related Lubricating Behaviors of α-Amylase on a Glass Surface
title Quantify the Protein–Protein Interaction Effects on Adsorption Related Lubricating Behaviors of α-Amylase on a Glass Surface
title_full Quantify the Protein–Protein Interaction Effects on Adsorption Related Lubricating Behaviors of α-Amylase on a Glass Surface
title_fullStr Quantify the Protein–Protein Interaction Effects on Adsorption Related Lubricating Behaviors of α-Amylase on a Glass Surface
title_full_unstemmed Quantify the Protein–Protein Interaction Effects on Adsorption Related Lubricating Behaviors of α-Amylase on a Glass Surface
title_short Quantify the Protein–Protein Interaction Effects on Adsorption Related Lubricating Behaviors of α-Amylase on a Glass Surface
title_sort quantify the protein–protein interaction effects on adsorption related lubricating behaviors of α-amylase on a glass surface
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7463787/
https://www.ncbi.nlm.nih.gov/pubmed/32722491
http://dx.doi.org/10.3390/polym12081658
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