Interfacial Complexes between a Protein and Lipophilic Ions at an Oil-Water Interface

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.


Published in:
Analytical Chemistry -Washington DC-, 82, 18, 7699–7705
Year:
2010
Publisher:
American Chemical Society
ISSN:
0003-2700
Keywords:
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 Record created 2011-05-11, last modified 2018-03-17

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