Effect of surface wettability on ion-specific protein adsorption.

We have systematically investigated the effect of surface wettability on ion-specific adsorption of bovine serum albumin (BSA) by using quartz crystal microbalance with dissipation (QCM-D) and surface plasmon resonance (SPR). The changes in frequency (Δf) and resonance unit (ΔRU) show a nonmonotonous change of the adsorbed amount of BSA as a function of molar fraction of 1-dodecanethiol (x(DDT)) of the self-assembled monolayer at pH 3.8, while the amount of adsorbed protein gradually increases with the x(DDT) at pH 7.4. The small changes of dissipation (ΔD) indicate that BSA molecules form a quite rigid protein layer on the surfaces, which results in only a slight difference in the adsorbed mass between the mass-uptake estimations from the Sauerbrey equation and the Voigt model. The difference in the adsorbed mass between QCM-D and SPR measurements is attributed to the coupled water in the protein layer. On the other hand, specific anion effect is observed in the BSA adsorption at pH 3.8 with the exception of the surface at x(DDT) of 0%, but no obvious cation specificity can be observed at pH 7.4. The ΔD-Δf plots show that the BSA adsorption at pH 3.8 has two distinct kinetic processes. The first one dominated by the protein-surface interactions is an anion-nonspecific process, whereas the second one dominated by the protein structural rearrangements is an anion-specific process. At pH 7.4, the second kinetic process can only be observed at the relatively hydrophobic surfaces, and no cation specificity is observed in the first and second kinetic processes.