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

TY - JOUR

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

U2 - 10.1021/ac101528r

DO - 10.1021/ac101528r

M3 - Journal article

C2 - 20735009

SN - 0003-2700

VL - 82

SP - 7699

EP - 7705

JO - Industrial And Engineering Chemistry Analytical Edition

JF - Industrial And Engineering Chemistry Analytical Edition

IS - 18

ER -