Reversibility of the adsorption of lysozyme on silica.

A central paradigm that underpins our understanding of the interaction of proteins with solid surfaces is that protein adsorption leads to changes in secondary structure. The bound proteins tend to denature, and these non-native, adsorbed structures are likely stabilized through the loss of α-helices with the concomitant formation of intermolecular β-sheets. The goal of this work is to critically assess the impact this behavior has on protein desorption, where irreversible conformational changes might lead to protein aggregation or result in other forms of instability. The adsorption, desorption, and structural transitions of lysozyme are examined on fumed silica nanoparticles as a function of the amount of protein adsorbed. Surprisingly, the data indicate not only that adsorption is reversible but also that protein desorption is predictable in a coverage-dependent manner. Additionally, there is evidence of a two-state model which involves exchange between a native-like dissolved state and a highly pertur...