Protein Adsorption Tuned by Multivalent Ions (PATMI):Connecting Bulk to Interface Behaviour by Controlling Interactions

本研究的目的是利用蛋白质溶液丰富的体相行为，包括多价离子介导的重入凝聚，来阐明蛋白质在界面吸附的基本原理，而不仅仅是简单的电荷屏蔽。（即吸附等温线将沿着平衡结构确定）和动态地（因此在平衡之前，即将研究吸附动力学），特别注意阐明表面诱导成核的作用及其对蛋白质结晶的重要性。我们的目标是将界面行为与多价离子控制的相互作用和离子概念内的本体行为联系起来。我们利用我们在表面分析技术方面的专业知识，如椭圆偏振法、QCM-D、FTIRRAS/ATR，特别是中子和X射线散射，可以在分子水平上详细确定吸附层结构。

This proposal aims to employ the rich bulk phase behaviour of protein solutions including re-entrant condensation mediated by multivalent ions to elucidate the fundamentals of protein adsorption at interfaces beyond simple charge screening.This qualitatively new behaviour will be explored both at equilibrium (i.e. adsorption isotherms will be determined along with the equilibrium structures) and dynamically (and therefore prior to equilibrium, i.e. the adsorption kinetics will be investigated), with particular attention to clarify the role of surface-induced nucleation and its importance for protein crystallisation.We aim to connect the interface behaviour to the interactions controlled by multivalent ions and the bulk behaviour within the concept of ion-activated patches.We make use of our expertise in surface analysis techniques, such as ellipsometry, QCM-D, FTIRRAS/ATR and in particular neutron and X-ray scattering, which allow a detailed determination of the adsorbed layer structure at the molecular level.