A nano LC-MALDI mass spectrometry droplet interface for the analysis of complex protein samples
A nano LC-MALDI mass spectrometry droplet interface for the analysis of complex protein samples
The integration of matrix-assisted laser desorption ionization (MALDI) mass spectrometry with an upstream analytical separations (such as liquid chromatography and electrophoresis) has opened up new opportunities for the automated investigation of complex protein and peptide mixtures. The ability to efficiently analyze complex proteomic mixtures in this manner is primarily determined by the ability to preserve spatial discrimination of sample components as they leave the separation column. Current interfacing methods are problematic in this respect since minimum fraction volumes are limited to several microliters. Herein we show for the first time an LC-MALDI interface based on the formation, processing and destruction of a segmented flow. The interface consists of a droplet-generator to fractionate LC effluent into nL-volume droplets and a deposition probe that transfers the sample (and MALDI matrix) onto a conventional MALDI-MS target. The efficacy of the method is demonstrated through the analysis of Trypsin digests of both BSA and Cytochrome C, with a 50% enhancement in analytical performance when compared to conventional interface technology.
e63087
Pereira, Fiona
018dd1e3-2e9a-4a2a-beeb-4f6b787808d5
Niu, Xize
f3d964fb-23b4-45db-92fe-02426e4e76fa
deMello, Andrew J.
ce9901e2-3de2-4fb8-a816-6917c578c582
Vertessy, Beata G.
62d6f288-10ac-4955-b5cd-4383d4226b0e
9 May 2013
Vertessy, Beata G.
62d6f288-10ac-4955-b5cd-4383d4226b0e
Pereira, Fiona
018dd1e3-2e9a-4a2a-beeb-4f6b787808d5
Niu, Xize
f3d964fb-23b4-45db-92fe-02426e4e76fa
deMello, Andrew J.
ce9901e2-3de2-4fb8-a816-6917c578c582
Pereira, Fiona, Niu, Xize and deMello, Andrew J.
,
Vertessy, Beata G.
(ed.)
(2013)
A nano LC-MALDI mass spectrometry droplet interface for the analysis of complex protein samples.
PLoS ONE, 8 (5), .
(doi:10.1371/journal.pone.0063087).
Abstract
The integration of matrix-assisted laser desorption ionization (MALDI) mass spectrometry with an upstream analytical separations (such as liquid chromatography and electrophoresis) has opened up new opportunities for the automated investigation of complex protein and peptide mixtures. The ability to efficiently analyze complex proteomic mixtures in this manner is primarily determined by the ability to preserve spatial discrimination of sample components as they leave the separation column. Current interfacing methods are problematic in this respect since minimum fraction volumes are limited to several microliters. Herein we show for the first time an LC-MALDI interface based on the formation, processing and destruction of a segmented flow. The interface consists of a droplet-generator to fractionate LC effluent into nL-volume droplets and a deposition probe that transfers the sample (and MALDI matrix) onto a conventional MALDI-MS target. The efficacy of the method is demonstrated through the analysis of Trypsin digests of both BSA and Cytochrome C, with a 50% enhancement in analytical performance when compared to conventional interface technology.
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Published date: 9 May 2013
Organisations:
Mechatronics
Identifiers
Local EPrints ID: 352564
URI: http://eprints.soton.ac.uk/id/eprint/352564
ISSN: 1932-6203
PURE UUID: 5629434b-423f-41d0-9c8e-2d388d4588ea
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Date deposited: 16 May 2013 10:47
Last modified: 14 Mar 2024 13:53
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Contributors
Editor:
Beata G. Vertessy
Author:
Fiona Pereira
Author:
Andrew J. deMello
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