Biocompatible Materials Based on Self-Assembling Peptides on Ti25Nb1OZr Alloy: Molecular Structure and Organization Investigated by Synchrotron Radiation Induced Techniques
Abstract
In this work, we applied advanced Synchrotron Radiation (SR) induced techniques to the study of the chemisorption of the Self Assembling Peptide EAbuK16, i.e., H-Abu-Glu-Abu-Glu-Abu-Lys-Abu-Lys-Abu-Glu-Abu-Glu-Abu-Lys-Abu-Lys-NH2 that is able to spontaneously aggregate in anti-parallel P-sheet conformation, onto annealed Ti25NblOZr alloy surfaces. This synthetic amphiphilic oligopeptide is a good candidate to mimic extracellular matrix for bone prosthesis, since its beta-sheets stack onto each other in a multilayer oriented nanostructure with internal pores of 5-200 nm size.
To prepare the biomimetic material, Ti25NblOZr discs were treated with aqueous solutions of EAbuK16 at different pH values. Here we present the results achieved by performing SR-induced X-ray Photoelectron Spectroscopy (SR-XPS), angle-dependent Near Edge X-ray Absorption Fine Structure (NEXAFS) spectroscopy, FESEM and AFM imaging on Ti25NblOZr discs after incubation with self-assembling peptide solution at five different pH values, selected deliberately to investigate the best conditions for peptide immobilization.