Fibronectin adsorption on tantalum: the influence of nanoroughness.
The complex mechanisms of protein adsorption at the solid-liquid interface is of great importance in many research areas, including protein purification, biocompatibility of medical implants, biosensing, and biofouling. The protein adsorption process depends crucially on both the nanoscale chemistry and topography of the interface. Here, we investigate the adsorption of the cell-binding protein fibronectin on flat and nanometer scale rough tantalum oxide surfaces using ellipsometry and quartz crystal microbalance with dissipation (QCM-D). On the flat tantalum oxide surfaces, the interfacial protein spreading causes an increase in the rigidity and a decrease in the thickness of the adsorbed fibronectin layer with decreasing bulk protein concentration. For the tantalum oxide surfaces with well-controlled, stochastic nanometer scale roughness, similar concentration effects are observed for the rigidity of the fibronectin layer and saturated fibronectin uptake. However, we find that the nanorough tantalum oxide surfaces promote additional protein conformational changes, an effect especially apparent from the QCM-D signals, interpreted as an additional stiffening of the formed fibronectin layers.
Hovgaard
Mads Bruun
MB
Interdisciplinary Nanoscience Center (iNANO) and Department of Physics and Astronomy, University of Aarhus, DK-8000 Aarhus C, Denmark.
Rechendorff
Kristian
K
Chevallier
Jacques
J
Foss
Morten
M
Besenbacher
Flemming
F
D000327:Adsorption; D000906:Antibodies / Q000276:immunology; D003460:Crystallization; D005353:Fibronectins / Q000737:chemistry* / Q000276:immunology / Q000648:ultrastructure; D006801:Humans; D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D010087:Oxides / Q000737:chemistry; D013499:Surface Properties; D013635:Tantalum / Q000737:chemistry*
D000906:Antibodies; D005353:Fibronectins; D010087:Oxides; D013635:Tantalum