Interfacial Complexes between a Protein and Lipophilic Ions at an Oil-Water Interface
Interfacial Complexes between a Protein and Lipophilic Ions at an Oil-Water Interface
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DOI：
10.1021/ac101528r
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发表时间：
2010-09-15
影响因子：
7.4
通讯作者：
Jensen, Henrik
中科院分区：
文献类型：
--
作者：
Hartvig, Rune A.;Mendez, Manuel A.;Jensen, Henrik
采用循环伏安法、阻抗技术和一种新开发的双相电喷雾质谱（BESI-MS）分析方法，研究了油水界面上完整蛋白质和两种亲脂性离子之间的相互作用。结果发现，蛋白质形成界面复合物与亲脂性离子，它特别需要的存在下，在实验条件下形成的油-水界面。此外，基于阻抗的技术和BESI-MS与一个共同的离子来表征界面表明，跨油-水界面的伽伐尼电位差显着影响界面络合程度。因此，能够调查蛋白质配体复合物形成的极化液-液界面是一种新的分析方法，用于评估潜在的依赖性界面络合使用的结构阐明检测原理。
The interaction between an intact protein and two lipophilic ions at an oil water interface has been investigated using cyclic voltammetry, impedance based techniques and a newly developed method in which the biphasic oil water system is analyzed by biphasic electrospray ionization mass spectrometry (BESI-MS), using a dualchannel electrospray emitter. It is found that the protein forms interfacial complexes with the lipophilic ions and that it specifically requires the presence of the oil water interface to be formed under the experimental conditions. Furthermore, impedance based techniques and BESI-MS with a common ion to polarize the interface indicated that the Galvani potential difference across the oil water interface significantly influences the interfacial complexation degree. The ability to investigate protein ligand complexes formed at polarized liquid liquid interfaces is thus a new analytical method for assessing potential dependent interfacial complexation using a structure elucidating detection principle.