The Role of the Hydrophobic Effect in Protein Adsorption

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The hypothesis that proteins in aqueous solution interact with adsorbent surfaces primarily via hydrophobic interactions will be tested by manipulation of the hydrophobic effect at its origin: the ability of the solvent to assume ordered structures in the vicinity of nonpolar species. This method is a desirable alternative to studies of protein adsorption to a wide variety of materials, where aspects of the surface chemistry other than hydrophobicity are varied in an uncontrolled manner. As cosolvents with water, methanol impairs the hydrophobic effect, glycerol enhances it, and ethylene glycol does not significantly alter the effect. By careful selection of the experimental system, constant protein conformation and adsorbent surface chemistry will be maintained in the presence of the different structure- altering cosolvents in order to assess the role of the hydrophobic effect in controlling adsorption isotherms and rates, adsorption reversibility, and surface diffusion. While adsorption isotherms and rates of adsorption and desorption reflect long time processes, measurements of surface diffusion coefficients provide information about processes occurring in the protein-surface binding region on rapid time scales.