Interfacial complexes between a protein and lipophilic ions at an oil - water interface

Rune Andersen Hartvig; Manuel A. Méndez; Marco van de Weert; Lene Jørgensen; Jesper Østergaard; Hubert H. Girault; Henrik Jensen

doi:10.1021/ac101528r

Interfacial complexes between a protein and lipophilic ions at an oil - water interface

Rune Andersen Hartvig, Manuel A. Méndez, Marco van de Weert, Lene Jørgensen, Jesper Østergaard, Hubert H. Girault, Henrik Jensen

43 Citations (Scopus)

Abstract

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 dual-channel 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.

Original language	English
Journal	Analytical Chemistry
Volume	82
Issue number	18
Pages (from-to)	7699-7705
ISSN	0003-2700
DOIs	https://doi.org/10.1021/ac101528r
Publication status	Published - 15 Sept 2010

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Former Faculty of Pharmaceutical Sciences

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10.1021/ac101528r

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title = "Interfacial complexes between a protein and lipophilic ions at an oil - water interface",

abstract = "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 dual-channel 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.",

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T1 - Interfacial complexes between a protein and lipophilic ions at an oil - water interface

AU - Hartvig, Rune Andersen

AU - Méndez, Manuel A.

AU - van de Weert, Marco

AU - Jørgensen, Lene

AU - Østergaard, Jesper

AU - Girault, Hubert H.

AU - Jensen, Henrik

PY - 2010/9/15

Y1 - 2010/9/15

N2 - 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 dual-channel 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.

AB - 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 dual-channel 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.

KW - Former Faculty of Pharmaceutical Sciences

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JO - Industrial And Engineering Chemistry Analytical Edition

JF - Industrial And Engineering Chemistry Analytical Edition

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Interfacial complexes between a protein and lipophilic ions at an oil - water interface

Abstract

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