Surface characteristics and protein adsorption on combinatorial binary Ti-M (Cr, Al, Ni) and Al-M (Ta, Zr) library films

Systematic studies of protein adsorption onto metallic biomaterial surfaces are generally lacking. Here, combinatorial binary library films with compositional gradients of Ti1-xCrx, Ti1-xAlx, Ti1-xNix and Al1-xTax, (0 < x < 1) and Al1-yZry (0 < y < 0.5) as well as corresponding pure metal films were sputtered onto clean Si surfaces. Bulk and surface chemistry, film microstructure, and surface roughness were subsequently correlated to fibrinogen or albumin adsorption measured using a high throughput wavelength dispersive spectroscopy technique. X-ray diffraction revealed these binary films to have crystalline phases present primarily at either extreme of the compositional library and an amorphous zone dominating along the gradient. These mirror-like films were generally found by atomic force microscopy to have a roughness of less than 8 nm, with any relative increases in roughness consistent with the development of crystalline phases. Surface chemistry by quantitative high-resolution X-ray photoelectron spectroscopy differed significantly from bulk film composition as measured by electron microprobe, with TiO2 and Al2O3 preferentially forming on the binary film surfaces. Correspondingly, protein adsorption onto these films closely correlated with their surface oxide fractions. Aluminum deposited as either a constant-composition film or as part of a binary library consistently adsorbed the least amount of albumin and fibrinogen, with alumina-enrichment of the surface oxide correlating with this adsorption. Overall, this combinatorial materials approach coupled with high-throughput surface analytical methods provides an efficient method of screening potential metallic biomaterials that may enable as well systematic studies of surface properties driving protein adsorption on these metal / metal oxide systems. (C) 2009 Wiley Periodicals, Inc. J Biomed Mater Res 92A: 521-532, 2010