Enhancement of protein adsorption induced by surface roughness.

Using quartz crystal microbalance with dissipation and ellipsometry, we show that during adsorption of fibrinogen on evaporated tantalum films the saturation uptake increases with increasing root-mean-square roughness (from 2.0 to 32.9 nm) beyond the accompanying increase in surface area. This increase is attributed to a change in the geometrical arrangement of the fibrinogen molecules on the surface. For comparison, the adsorption of a nearly globular protein, bovine serum albumin, was studied as well. In this case, the adsorption was less influenced by the roughness. Simple Monte Carlo simulations taking into account surface roughness and the anisotropic shape of fibrinogen reproduce the experimentally observed trend.