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

这个建议旨在利用蛋白质溶液丰富的体相行为，包括由多价离子介导的折入缩合，来阐明蛋白质在界面上吸附的基本原理，而不是简单的电荷筛选。这一定性的新行为将在平衡(即吸附等温线将与平衡结构一起确定)和动态(因此在平衡之前，即吸附动力学将被研究)两个方面进行探索。特别要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激活斑块的整体行为联系起来。我们利用我们在表面分析技术方面的专业知识，如椭偏仪、QCM-D、FTIRRAS/ATR，特别是中子和X射线散射，这些技术允许在分子水平上详细确定吸附的层结构。

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.