The Role of the Hydrophobic Effect in Protein Adsorption

蛋白质在水溶液中主要通过疏水相互作用与吸附表面相互作用的假设将通过对其起源的疏水效应的操纵来检验：溶剂在非极性物种附近呈现有序结构的能力。这种方法是研究蛋白质在各种材料上吸附的理想替代方法，在这些材料中，除疏水性之外的表面化学方面的变化是不受控制的。作为与水的共溶剂，甲醇会削弱疏水效果，甘油会增强疏水效果，而乙二醇则不会显著改变这种效果。通过仔细选择实验体系，在不同结构改变的助溶剂存在的情况下，保持恒定的蛋白质构象和吸附表面化学，以评估疏水效应在控制吸附等温线和速率、吸附可逆性和表面扩散中的作用。虽然吸附等温线和吸附和解吸速率反映了长时间的过程，但表面扩散系数的测量提供了快速时间尺度上发生在蛋白质表面结合区的过程的信息。

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.