Design and performance of a universal sheathless capillary electrophoresis to mass spectrometry interface using a split-flow technique.
A split-flow capillary electrophoresis electrospray ionization mass spectrometry (CE/ESI-MS) interface is introduced, in which the electrical connection to the CE capillary outlet is achieved by diverting part of the CE buffer out of the capillary through an opening near the capillary outlet. The CE buffer exiting the opening contacts a sheath metal tube which acts as the CE outlet/ESI shared electrode. In cases in which the ESI source uses a metal needle, the voltage contact to the CE buffer is achieved by simply inserting the outlet of the CE capillary, which contains an opening, into the existing ESI needle (thereby greatly simplifying the CE to MS interfacing). As a result of the concentration-sensitive nature of ESI, splitting a small percentage of the CE flow has minimal effect on the sensitivity of detection. In addition, because the liquid is flowing through the opening and out of the capillary, there is no dead volume associated with this interface. Moreover, bubble formation due to redox reactions of water at the electrode does not effect CE/ESI-MS performance, because the actual metal/liquid contact occurs outside of the CE capillary. The sensitivity associated with a sheathless CE/MS interface, the ease of fabrication, universality, and lack of any dead volume make this design a superior CE/ESI-MS interface. The performance of this interface is demonstrated by analyses of a peptide standard and a protein digest using a variety of capillary dimensions.
Moini
M
M
Department of Chemistry and Biochemistry, The University of Texas at Austin, 78712, USA. mmoini@mail.utexas.edu
D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000032:analysis; D019075:Electrophoresis, Capillary / Q000379:methods*; D010446:Peptide Fragments / Q000032:analysis; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*
D003574:Cytochrome c Group; D010446:Peptide Fragments