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

Author:

Secchi ValeriaORCID,Franchi StefanoORCID,Dettin MonicaORCID,Zamuner Annj,Beranová KláraORCID,Vladescu AlinaORCID,Battocchio ChiaraORCID,Graziani ValerioORCID,Tortora LucaORCID,Iucci GiovannaORCID

Abstract

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.

Publisher

MDPI AG

Subject

General Materials Science,General Chemical Engineering

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