Bovine serum albumin adsorption on nano-rough platinum surfaces studied by QCM-D

• Published in: Colloids and surfaces, B, Biointerfaces Vol. 66; no. 1; pp. 53 - 59
• Main Authors: Dolatshahi-Pirouz, A., Rechendorff, K., Hovgaard, M.B., Foss, M., Chevallier, J., Besenbacher, F.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.10.2008
• Subjects: Adsorption; Animals; BSA; Cattle; Coated Materials, Biocompatible - chemistry; Immunoglobulin G - metabolism; Metal Nanoparticles - chemistry; Microscopy, Atomic Force; Nano-topography; Platinum; Platinum - chemistry; Platinum - metabolism; Protein adsorption; QCM-D; Quartz - chemistry; Serum Albumin, Bovine - chemistry; Serum Albumin, Bovine - metabolism; Surface Properties; BSA; Nano-topography; Platinum; Protein adsorption; QCM-D
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2008.05.010

The adsorption of bovine serum albumin (BSA) on platinum surfaces with a root-mean-square roughness ranging from 1.49 nm to 4.62 nm was investigated using quartz crystal microbalance with dissipation (QCM-D). Two different BSA concentrations, 50 μg/ml and 1 mg/ml, were used, and the adsorption studies were complemented by monitoring the antibody interaction with the adsorbed BSA layer. The adsorption process was significantly influenced by the surface nano-roughness, and it was observed that the surface mass density of the adsorbed BSA layer is enhanced in a non-trivial way with the surface roughness. From a close examination of the energy dissipation vs. frequency shift plot obtained by the QCM-D technique, it was additionally observed that the BSA adsorption on the roughest surface is subject to several distinct adsorption phases revealing the presence of structural changes facilitated by the nano-rough surface morphology during the adsorption process. These changes were in particular noticeable for the adsorption at the low (50 μg/ml) BSA concentration. The results confirm that the nano-rough surface morphology has a significant influence on both the BSA mass uptake and the functionality of the resulting protein layer.