Effects of Pressure on the Adsorption of Proteins at Aqueous-Solid Interfaces

Abstract

The spontaneous adsorption of proteins at aqueous-solid interfaces plays an important role in nature, medicine, and biotechnology. A sound understanding of the molecular mechanisms and interactions upon protein adsorption is required for the development of new materials coatings and for the choice of solvent conditions. So far, protein adsorption studies have been carried out mainly as a function of protein solution concentration, pH-value, and surface chemistry. In addition, several temperature-dependent studies have shed some light on the thermodynamics underlying protein adsorption. In contrast, effects of pressure on this process are widely unknown. Applying pressure to molecular systems generally offers access to all kinds of volume changes occurring during assembly of molecules, phase transitions, and chemical reactions. In the case of protein adsorption, using pressure as a thermodynamic variable allows for the determination of volume changes of adsorption, volume changes of unfolding in the adsorbed state, and changes of protein-interface interactions that determine the degree of protein adsorption. We have designed new high pressure cells for total internal reflection fluorescence (TIRF) spectroscopy and neutron reflectometry (NR) for pressures up to 2500 bar in order to access these quantities. The results obtained so far indicate a pressure-induced increase of the degree of protein adsorption at both the water-silica and water-poly(styrene) interfaces. Moreover, a drastic decrease of the volume change of unfolding has been found when proteins are adsorbed at the water-silica interface. Apparently, pressure exerts a distinct influence on the process of protein adsorption and provides a new complemental view on the underlying mechanism.