Amount and surface structure of albumin adsorbed to solid substrata with different wettabilities in a parallel plate...

In this article we studied the adsorption of serum albumin to substrata with a broad range of wettabilities from solutions with protein concentrations between 0.03 and 3.00 mg.mL-1 in a parallel-plate flow cell. Wall shear rates were varied between 20 and 2000 s-1. The amount of albumin adsorbed in a stationary state was always highest on PTFE, the most hydrophobic material employed and decreased with increasing wettability of the substrata. Increasing stationary amounts of adsorbed albumin were observed with increasing wall shear rates at the lowest protein concentration. Inverse observations were made at the highest protein concentration. Transmission electron micrographs of replicas from the albumin-coated substrata showed that proteins were mostly adsorbed in islandlike structures on the hydrophobic substrata. The tendency to form islandlike structures was shear rate- and concentration-dependent and disappeared gradually going to more hydrophilic substrata. On glass, the most hydrophilic material employed, a homogeneous, well distributed, fine knotted, reticulated structure was found. In conclusion, this study demonstrates that both the amount of adsorbed albumin as well as the surface structure of the adsorbed proteins are regulated by the substratum wettability. This observation may well account for the fact that substratum properties can be transferred by an adsorbed protein film to the interface with adhering cells or microorganisms.