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Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface to Provide Robust Corrosion Inhibition and Enhance In Vitro Osteo-Inductivity

Herein, we describe precisely a covalent modification of pure magnesium (Mg) surface and its application to induce in vitro osteogenic differentiation. The new concept of a chemical bonding method is proposed for developing stable chemical bonds on the Mg surface through the serial assembly of bioac...

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Autores principales: Lee, Seo Yeon, Shrestha, Sita, Shrestha, Bishnu Kumar, Park, Chan Hee, Kim, Cheol Sang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7077681/
https://www.ncbi.nlm.nih.gov/pubmed/32069827
http://dx.doi.org/10.3390/polym12020439
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author Lee, Seo Yeon
Shrestha, Sita
Shrestha, Bishnu Kumar
Park, Chan Hee
Kim, Cheol Sang
author_facet Lee, Seo Yeon
Shrestha, Sita
Shrestha, Bishnu Kumar
Park, Chan Hee
Kim, Cheol Sang
author_sort Lee, Seo Yeon
collection PubMed
description Herein, we describe precisely a covalent modification of pure magnesium (Mg) surface and its application to induce in vitro osteogenic differentiation. The new concept of a chemical bonding method is proposed for developing stable chemical bonds on the Mg surface through the serial assembly of bioactive additives that include ascorbic acid (AA) and bovine serum albumin (BSA). We studied both the physicochemical and electrochemical properties using scanning electron microscopy and other techniques to confirm how the covalent bonding of BSA on Mg can, after coating, significantly enhance the chemical stability of the substrate. The modified Mg-OH-AA-BSA exhibits better anti-corrosion behavior with high corrosion potential (E(corr) = −0.96 V) and low corrosion current density (I(corr) = 0.2 µA cm(−2)) as compared to the pure Mg (E(corr) = −1.46 V, I(corr) = 10.42 µA cm(−2)). The outer layer of BSA on Mg protects the fast degradation rate of Mg, which is the consequence of the strong chemicals bonds between amine groups on BSA with carboxylic groups on AA as the possible mechanism of peptide bonds. Collectively, the results suggest that the surface-modified Mg provides a strong bio-interface, and enhances the proliferation and differentiation of pre-osteoblast (MC3T3-E1) cells through a protein–lipid interaction. We therefore conclude that the technique we describe provides a cost-effective and scalable way to generate chemically stable Mg surface that inherits a biological advantage in orthopedic and dental implants in clinical applications.
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spelling pubmed-70776812020-03-20 Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface to Provide Robust Corrosion Inhibition and Enhance In Vitro Osteo-Inductivity Lee, Seo Yeon Shrestha, Sita Shrestha, Bishnu Kumar Park, Chan Hee Kim, Cheol Sang Polymers (Basel) Article Herein, we describe precisely a covalent modification of pure magnesium (Mg) surface and its application to induce in vitro osteogenic differentiation. The new concept of a chemical bonding method is proposed for developing stable chemical bonds on the Mg surface through the serial assembly of bioactive additives that include ascorbic acid (AA) and bovine serum albumin (BSA). We studied both the physicochemical and electrochemical properties using scanning electron microscopy and other techniques to confirm how the covalent bonding of BSA on Mg can, after coating, significantly enhance the chemical stability of the substrate. The modified Mg-OH-AA-BSA exhibits better anti-corrosion behavior with high corrosion potential (E(corr) = −0.96 V) and low corrosion current density (I(corr) = 0.2 µA cm(−2)) as compared to the pure Mg (E(corr) = −1.46 V, I(corr) = 10.42 µA cm(−2)). The outer layer of BSA on Mg protects the fast degradation rate of Mg, which is the consequence of the strong chemicals bonds between amine groups on BSA with carboxylic groups on AA as the possible mechanism of peptide bonds. Collectively, the results suggest that the surface-modified Mg provides a strong bio-interface, and enhances the proliferation and differentiation of pre-osteoblast (MC3T3-E1) cells through a protein–lipid interaction. We therefore conclude that the technique we describe provides a cost-effective and scalable way to generate chemically stable Mg surface that inherits a biological advantage in orthopedic and dental implants in clinical applications. MDPI 2020-02-13 /pmc/articles/PMC7077681/ /pubmed/32069827 http://dx.doi.org/10.3390/polym12020439 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
Lee, Seo Yeon
Shrestha, Sita
Shrestha, Bishnu Kumar
Park, Chan Hee
Kim, Cheol Sang
Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface to Provide Robust Corrosion Inhibition and Enhance In Vitro Osteo-Inductivity
title Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface to Provide Robust Corrosion Inhibition and Enhance In Vitro Osteo-Inductivity
title_full Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface to Provide Robust Corrosion Inhibition and Enhance In Vitro Osteo-Inductivity
title_fullStr Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface to Provide Robust Corrosion Inhibition and Enhance In Vitro Osteo-Inductivity
title_full_unstemmed Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface to Provide Robust Corrosion Inhibition and Enhance In Vitro Osteo-Inductivity
title_short Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface to Provide Robust Corrosion Inhibition and Enhance In Vitro Osteo-Inductivity
title_sort covalent surface functionalization of bovine serum albumin to magnesium surface to provide robust corrosion inhibition and enhance in vitro osteo-inductivity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7077681/
https://www.ncbi.nlm.nih.gov/pubmed/32069827
http://dx.doi.org/10.3390/polym12020439
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