Protein adsorption has a central role in the outcome of implants. However, there is no consensus about the impact of the different surface properties on the material-protein interactions. Here, the adsorption of albumin and fibronectin in near-physiological concentration is investigated on three differently treated titanium-based surfaces and compared after a thorough characterization. The different titanium surfaces have very different surface properties, in particular regarding roughness, oxide porosity, wettability, surface energy, and zeta potential, which are all known to deeply affect protein adsorption. By merging several characterization techniques, some conventional and some innovative, it was possible to discriminate the effect of surface properties on different aspects of protein adsorption. Despite forming a continuous layer on all samples, the amount of proteins bound to the surface is mainly due to surface roughness and topography, which can overcome the effect of wettability and surface energy. On the other hand, the secondary structure of albumin and fibronectin and their orientation are determined by the hydroxyl groups exposed on the surfaces, depending on their surface concentration and acidic reactivity in the former, and the surface zeta potential in the latter.

蛋白质吸附在植入物的结果中起着核心作用。然而，对于不同表面性质对材料-蛋白质相互作用的影响，目前还没有达成共识。在这里，在三种不同处理的钛基表面上研究了接近生理浓度的白蛋白和纤连蛋白的吸附，并在彻底表征后进行了比较。不同的钛表面具有非常不同的表面特性，特别是在粗糙度、氧化物孔隙率、润湿性、表面能和 zeta 电位方面，众所周知，这些都会深刻影响蛋白质的吸附。通过合并几种表征技术，一些传统的和一些创新的，可以区分表面性质对蛋白质吸附不同方面的影响。尽管在所有样品上都形成了连续层，但与表面结合的蛋白质数量主要是由于表面粗糙度和形貌，可以克服润湿性和表面能的影响。另一方面，白蛋白和纤连蛋白的二级结构和它们的取向由暴露在表面上的羟基决定，取决于它们的表面浓度和前者的酸性反应性，以及后者的表面zeta电位。