Nano-size protein at the surface of a Ti–Zr–Ni quasi-crystalline alloy: Fibronectin adsorption on metallic nano-composites

Abstract

Surface characterisation of alloys before and after their interaction with proteins allows a more rational design of biomaterials. In this work, fibronectin adsorption on a Ti-based quasicrystals-forming alloy was studied by X-ray photoelectron spectroscopy (XPS) and compared to those obtained on pure titanium substrates (cp Ti). Different fibronectin (Fn) solution concentrations were tested in interaction with the quasi-crystalline/amorphous Ti45Zr38Ni17 composite. N 1s, C 1s, Ti 2p, Zr 3d and Ni 2p core level spectra were systematically recorded. The results indicate that fibronectin is chemically adsorbed on Ti45Zr38Ni17 as well as on cp Ti. The alloy surface composition and oxide thickness are not significantly changed in presence of the adsorbed protein. Data on the elemental distribution in the alloy surface obtained by XPS were completed by depth profiling with Time of Flight Secondary Ion Mass Spectrometry (ToF-SIMS). Surface saturation is clearly reached for Fn solution concentrations of 100–150μgmL−1 for both surfaces. On the plateau, the equivalent protein thickness is 6nm for Ti45Zr38Ni17 and 8nm for cp Ti, both corresponding to one fibronectin monolayer. These results are in accordance with previous observations on osteoblasts adhesion, confirming the biocompatibility of Ti45Zr38Ni17. However, quasicrystals do not seem to influence the alloy surface reactivity.