The nanoscale surface topography of biomaterials can have strong effects on protein adsorption. While there are numerous surface statistical parameters for the characterization of nanorough surfaces, none of them alone provides a complete description of surface morphology. Herein, a selection of nanorough titanium oxide surfaces has been fabricated with root-mean-square roughness (Sq) values below 2.7 nm but very different surface morphologies. The adsorption of the proteins myoglobin (MGB), bovine serum albumin (BSA), and thyroglobulin (TGL) at these surfaces was investigated in situ by ellipsometry to assess the importance of six of the most common surface statistical parameters. For BSA adsorption, both protein film thickness and time constant of adsorption were found to scale linearly with Sq s. For TGL, however, the same adsorption characteristics depend linearly on the surface skewness (Ssk), which we attribute to the rather extreme size of this protein. Finally, a mixed behavior is observed for MGB adsorption, showing different linear correlations with Sq and Ssk. These results demonstrate the importance of a thorough morphological characterization of the surfaces employed in protein adsorption and possibly also cell adhesion studies.
Keywords: adsorption; atomic force microscopy; ellipsometry; surface roughness; surface topography.