INTEC   05402
INSTITUTO DE DESARROLLO TECNOLOGICO PARA LA INDUSTRIA QUIMICA
Unidad Ejecutora - UE
artículos
Título:
Column coupling isotachophoresiscapillary electrophoresis with mass spectrometric detection: Characterization and optimization of microfluidic interfaces
Autor/es:
KLER, PABLO A.; POSCH, TJORBEN N.; PATTKY, MARTIN; TIGGELAAR, ROALD M.; HUHN, CAROLIN
Revista:
JOURNAL OF CHROMATOGRAPHY - A
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Lugar: Amsterdam; Año: 2013 vol. 1297 p. 204 - 212
ISSN:
0021-9673
Resumen:
Two-dimensional electrophoretic separations are one of the most promising tools for the continuously
growing needs of different bioanalytical fields such as proteomics and metabolomics. In this work we
present the design and the implementation of a two-dimensional electrophoretic separation coupled
to mass spectrometry. We started our work studying the sample transfer characteristics of different
microfluidic interfaces compatible with capillary coupling for two-dimensional electrophoretic separations.
These junctions are aimed at method decoupling and sample transfer in a modular two-dimensional
electrophoretic separation system. In order to perform the characterization of the interfaces, we carried
out capillary electrophoresis experiments and numerical simulations using three cationic compounds
under different flow conditions. The comparison of the experimental and simulation results enables
us to clearly define the desirable characteristics of interfaces in order to achieve method orthogonality
with lossless sample transfer in a two-dimensional separation system. Finally, we present a glass
microfluidic chip as interface for the implementation of a novel hybrid modular system for performing
two-dimensional electrophoretic separations involving isotachophoresis and capillary electrophoresis.
In this setup we include mass spectrometric and contactless capacitively coupled conductivity detection
to monitor the separation process. We demonstrate the ability of the setup to be used as a flexible analysis
tool by performing preconcentration, separation, detection and identification of four different human
angiotensin peptides.