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Hydroxyapatite Surfaces Functionalized with a Self-Assembling Peptide: XPS, RAIRS and NEXAFS Study

Hydroxyapatite (HAP) coatings can improve the biocompatibility and bioactivity of titanium alloys, such as Ti6Al4V, commonly used as material for orthopedic prostheses. In this framework, we have studied the surface of HAP coatings enriched with Mg and either Si or Ti deposited by RF magnetron sputt...

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Autores principales: Secchi, Valeria, Franchi, Stefano, Dettin, Monica, Zamuner, Annj, Beranová, Klára, Vladescu, Alina, Battocchio, Chiara, Graziani, Valerio, Tortora, Luca, Iucci, Giovanna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7353169/
https://www.ncbi.nlm.nih.gov/pubmed/32545421
http://dx.doi.org/10.3390/nano10061151
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author Secchi, Valeria
Franchi, Stefano
Dettin, Monica
Zamuner, Annj
Beranová, Klára
Vladescu, Alina
Battocchio, Chiara
Graziani, Valerio
Tortora, Luca
Iucci, Giovanna
author_facet Secchi, Valeria
Franchi, Stefano
Dettin, Monica
Zamuner, Annj
Beranová, Klára
Vladescu, Alina
Battocchio, Chiara
Graziani, Valerio
Tortora, Luca
Iucci, Giovanna
author_sort Secchi, Valeria
collection PubMed
description Hydroxyapatite (HAP) coatings can improve the biocompatibility and bioactivity of titanium alloys, such as Ti6Al4V, commonly used as material for orthopedic prostheses. In this framework, we have studied the surface of HAP coatings enriched with Mg and either Si or Ti deposited by RF magnetron sputtering on Ti6Al4V. HAP coatings have been furtherly functionalized by adsorption of a self-assembling peptide (SAP) on the HAP surface, with the aim of increasing the material bioactivity. The selected SAP (peptide sequence AbuEAbuEAbuKAbuKAbuEAbuEAbuKAbuK) is a self-complementary oligopeptide able to generate extended ordered structures by self-assembling in watery solutions. Samples were prepared by incubation of the HAP coatings in SAP solutions and subsequently analyzed by X-ray Photoelectron Spectroscopy (XPS), Fourier Transform Infrared (FTIR) and Near Edge X-ray Absorption Fine Structure (NEXAFS) spectroscopies, in order to determine the amount of adsorbed peptide, the peptide stability and the structure of the peptide overlayer on the HAP coatings as a function of the HAP substrate and of the pH of the mother SAP solution. Experimental data yielded evidence of SAP adsorption on the HAP surface, and peptide overlayers showed ordered structure and molecular orientation. The thickness of the SAP overlayer depends on the composition of the HAP coating.
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spelling pubmed-73531692020-07-15 Hydroxyapatite Surfaces Functionalized with a Self-Assembling Peptide: XPS, RAIRS and NEXAFS Study Secchi, Valeria Franchi, Stefano Dettin, Monica Zamuner, Annj Beranová, Klára Vladescu, Alina Battocchio, Chiara Graziani, Valerio Tortora, Luca Iucci, Giovanna Nanomaterials (Basel) Article Hydroxyapatite (HAP) coatings can improve the biocompatibility and bioactivity of titanium alloys, such as Ti6Al4V, commonly used as material for orthopedic prostheses. In this framework, we have studied the surface of HAP coatings enriched with Mg and either Si or Ti deposited by RF magnetron sputtering on Ti6Al4V. HAP coatings have been furtherly functionalized by adsorption of a self-assembling peptide (SAP) on the HAP surface, with the aim of increasing the material bioactivity. The selected SAP (peptide sequence AbuEAbuEAbuKAbuKAbuEAbuEAbuKAbuK) is a self-complementary oligopeptide able to generate extended ordered structures by self-assembling in watery solutions. Samples were prepared by incubation of the HAP coatings in SAP solutions and subsequently analyzed by X-ray Photoelectron Spectroscopy (XPS), Fourier Transform Infrared (FTIR) and Near Edge X-ray Absorption Fine Structure (NEXAFS) spectroscopies, in order to determine the amount of adsorbed peptide, the peptide stability and the structure of the peptide overlayer on the HAP coatings as a function of the HAP substrate and of the pH of the mother SAP solution. Experimental data yielded evidence of SAP adsorption on the HAP surface, and peptide overlayers showed ordered structure and molecular orientation. The thickness of the SAP overlayer depends on the composition of the HAP coating. MDPI 2020-06-12 /pmc/articles/PMC7353169/ /pubmed/32545421 http://dx.doi.org/10.3390/nano10061151 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
Secchi, Valeria
Franchi, Stefano
Dettin, Monica
Zamuner, Annj
Beranová, Klára
Vladescu, Alina
Battocchio, Chiara
Graziani, Valerio
Tortora, Luca
Iucci, Giovanna
Hydroxyapatite Surfaces Functionalized with a Self-Assembling Peptide: XPS, RAIRS and NEXAFS Study
title Hydroxyapatite Surfaces Functionalized with a Self-Assembling Peptide: XPS, RAIRS and NEXAFS Study
title_full Hydroxyapatite Surfaces Functionalized with a Self-Assembling Peptide: XPS, RAIRS and NEXAFS Study
title_fullStr Hydroxyapatite Surfaces Functionalized with a Self-Assembling Peptide: XPS, RAIRS and NEXAFS Study
title_full_unstemmed Hydroxyapatite Surfaces Functionalized with a Self-Assembling Peptide: XPS, RAIRS and NEXAFS Study
title_short Hydroxyapatite Surfaces Functionalized with a Self-Assembling Peptide: XPS, RAIRS and NEXAFS Study
title_sort hydroxyapatite surfaces functionalized with a self-assembling peptide: xps, rairs and nexafs study
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7353169/
https://www.ncbi.nlm.nih.gov/pubmed/32545421
http://dx.doi.org/10.3390/nano10061151
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