Study on separation of protein molecules based on their selective

在特殊条件下处理的单晶蓝宝石表面表现出亲水性和疏水性的相分离。利用这个表面，我们研究了固体表面和生物分子之间的相互作用。为了明确畴表面的化学性质，我们使用了配备胶体探针的扫描探针显微镜，并测量了探针胶体与固体表面之间的附着力。我们观察到亲水性和疏水性结构域在化学状态上的明显差异。然后，我们研究了各种蛋白质分子的吸附机理，发现分子吸附的主要力量是静电力。但是，一些实验结果表明，疏水相互作用也参与了蛋白质吸附后的粘附。

Single-crystalline sapphire surfaces treated under particular conditions exhibit a phase separation into hydrophilic and hydrophobic domains. Using this surface, we have studied interactions between solid surfaces and biomolecules. To clarify the chemical properties of the domain surfaces, we used scanning probe microscopy equipped with colloidal probes and measured adhesion forces between the probe colloids and the solid surfaces. We observed distinct differences in the chemical states between the hydrophilic and the hydrophobic domains. Then, we investigated the adsorption mechanism of various protein molecules and found that the major force in the molecule adsorption is electrostatic one. But, some experimental results suggest that hydrophobic interaction is also involved in the adhesion of proteins after their adsorption.