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

多价离子调节的蛋白质吸附 (PATMI)：通过控制相互作用将体相与界面行为联系起来

• 批准号: 431858909
• 负责人: Professor Dr. Frank Schreiber
• 金额: --
• 依托单位: Lehrstuhl Physik der molekularen und biologischen Materie
• 依托单位国家: 德国
• 项目类别: Research Grants
• 资助国家: 德国
• 项目状态: 未结题
• 来源: https://gepris.dfg.de/gepris/projekt/431858909?language=en
• 关键词: Protein; Adsorption; Tuned; Multivalent; Ions

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.

该提案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重入冷凝，以阐明界面上蛋白质吸附的基本原理，而不仅仅是简单的电荷筛选。这种定性的新行为将在平衡状态（即吸附等温线将与平衡结构一起确定）和动态状态（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以及离子激活斑块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，例如椭圆光度法、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。