The Role of the Hydrophobic Effect in Protein Adsorption

假设水溶液中的蛋白质主要通过疏水相互作用与吸附剂表面相互作用，将通过在其起源处操纵疏水效应来验证：溶剂在非极性物质附近假设有序结构的能力。这种方法是研究蛋白质对各种材料吸附的理想替代方法，在这些材料中，表面化学的各个方面（疏水性除外）以一种不受控制的方式变化。作为水的共溶剂，甲醇削弱疏水效果，甘油增强疏水效果，乙二醇不显著改变疏水效果。通过仔细选择实验系统，在不同结构改变的共溶剂存在下，保持恒定的蛋白质构象和吸附剂表面化学性质，以评估疏水效应在控制吸附等温线和速率、吸附可逆性、表面扩散。吸附等温线和吸附和解吸速率反映了长时间的过程，而表面扩散系数的测量提供了在快速时间尺度上发生在蛋白质表面结合区域的过程的信息。

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.