By a News Reporter-Staff News Editor at Life Science Weekly -- Data detailed on Proteins have been presented. According to news reporting out of Paris, France, by NewsRx editors, research stated, "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)."
Our news journalists obtained a quote from the research from National Center for Scientific Research (CNRS), "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 100-150 mu g mL(-1) for both surfaces. On the plateau, the equivalent protein thickness is 6 nm for Ti45Zr38Ni17 and 8 nm 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."
According to the news editors, the research concluded: "However, quasicrystals do not seem to influence the alloy surface reactivity."
For more information on this research see: Nano-size protein at the surface of a Ti-Zr-Ni quasi-crystalline alloy: Fibronectin adsorption on metallic nano-composites. Colloids and Surfaces A-Physicochemical and Engineering Aspects, 2013;439():207-214. Colloids and Surfaces A-Physicochemical and Engineering Aspects can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands (see also Proteins).
Our news journalists report that additional information may be obtained by contacting H. Lefaix, Chim Paristech Ecole Natl Super Chim Paris, Lab Physicochim Surfaces, CNRS ENSCP UMR 7045, F-75005 Paris, France. Additional authors for this research include A. Galtayries, F. Prima and P. Marcus.
Keywords for this news article include: Paris, France, Europe, Fibronectins, Serum Globulins, Membrane Glycoproteins, Extracellular Matrix Proteins
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