蛋白分子与载体间相互作用，在不同条件下形成复杂多变的纳微界面，产生截然不同的性能，导致复杂界面现象，难以优化调控，故如何对蛋白分子与载体间作用进行普遍化描述是关键所在。本项目拟通过原子力显微镜AFM定量测定典型蛋白分子——牛血清蛋白，溶菌酶，肌红蛋白，卵清蛋白与介孔氧化钛载体界面间的作用粘附力和摩擦系数；利用对应状态原理普遍化方法从分子间作用出发，弄清蛋白分子-载体间作用与对比性质的普遍函数关系，探索典型蛋白与氧化钛载体界面间作用的普遍化规律，遴选关键控制因素；考察表面几何结构和溶液pH值所引起的范德华力和静电力变化对载体界面处蛋白分子行为差异的贡献；由AFM定量手段和对应状态原理普遍化方法共同关联分子间作用参数与载体界面蛋白分子行为的特征量“粘附力，摩擦系数，蛋白分子平衡吸附量，色谱保留时间”，借此描述和预测蛋白分子与载体间的作用行为，以期为色谱分离的优化调控提供指导。

The interactions of protein molecules with the support under different conditions, lead to the formation of complex nano/micro interfaces and, this will result in distinct interfacial performances as well as the complicated phenomena which is difficult to control and optimize. Therefore, how to describe protein-support interactions in generalized and quantitative manners is the key. In this project, the extensively studied proteins——Bovine Serum Albumin, Myoglobin, Lysozyme, and Ovalbumin will be chosen as the model proteins. We will employ the titanium dioxide substrate as a support, by using Atomic Force Microscopy (AFM), to study the protein-support interfacial forces, i.e. adhesion and friction coefficient. The corresponding states theory will be considered to analyze protein-TiO2 support interactions to find the universal function in terms of key dimensionless quantities and explore the generalized relationships. The protein adsorptive behaviour will be evaluated to confirm the dominant factor by varying TiO2 support geometries and pH conditions to adjust van der Waals and electrostatic interactions. Combining the quantitative AFM technique and generalized corresponding states theory analysis, the quantitative relationship between intermolecular forces and “adhesion, friction coefficient, the equilibrium amount of protein adsorption, the retention time” will be obtained. The findings will be expected to be employed to describe and predict various protein behaviour onto supports, to further guide the optimization of protein separation by chromatograph.