Detection and fragmentation of doubly charged peptide ions in MALDI-Q-TOF-MS by ion mobility spectrometry for improved protein identification.

Sproß J, Muck A, Gröger H (2019)
Analytical and bioanalytical chemistry 411(24): 1-11.

Zeitschriftenaufsatz | E-Veröff. vor dem Druck | Englisch
 
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Abstract / Bemerkung
Today, bottom-up protein identification in MALDI-MS is based on employing singly charged peptide ions, which are predominantly formed in the ionization process. However, peptide mass fingerprinting (PMF) with subsequent tandem MS confirmation using these peptide ions is often hampered due to the lower quality of fragment ion mass spectra caused by the higher collision energy necessary for fragmenting singly protonated peptides. Accordingly, peptide ions of higher charge states would be of high interest for analytical purposes, but they are usually not detected in MALDI-MS experiments as they overlap with singly charged matrix clusters and peptide ions. However, when utilizing ion mobility spectrometry (IMS), doubly charged peptide ions can be actively used by separating them from the singly protonated peptides, visualized, and selectively targeted for tandem MS experiments. The generated peptide fragment ion spectra can be used for a more confident protein identification using PMF with tandem MS confirmation, as most doubly protonated peptide ions yield fragment ion mass spectra of higher quality compared to tandem mass spectra of the corresponding singly protonated precursor ions. Mascot protein scores can be increased by approximately 50% when using tandem mass spectra of doubly charged peptide ions, with ion scores up to six times higher compared with ion scores of tandem mass spectra from singly charged precursors.
Erscheinungsjahr
2019
Zeitschriftentitel
Analytical and bioanalytical chemistry
Band
411
Ausgabe
24
Seite(n)
1-11
ISSN
1618-2642
eISSN
1618-2650
Page URI
https://pub.uni-bielefeld.de/record/2934545

Zitieren

Sproß J, Muck A, Gröger H. Detection and fragmentation of doubly charged peptide ions in MALDI-Q-TOF-MS by ion mobility spectrometry for improved protein identification. Analytical and bioanalytical chemistry. 2019;411(24):1-11.
Sproß, J., Muck, A., & Gröger, H. (2019). Detection and fragmentation of doubly charged peptide ions in MALDI-Q-TOF-MS by ion mobility spectrometry for improved protein identification. Analytical and bioanalytical chemistry, 411(24), 1-11. doi:10.1007/s00216-019-01578-8
Sproß, Jens, Muck, Alexander, and Gröger, Harald. 2019. “Detection and fragmentation of doubly charged peptide ions in MALDI-Q-TOF-MS by ion mobility spectrometry for improved protein identification.”. Analytical and bioanalytical chemistry 411 (24): 1-11.
Sproß, J., Muck, A., and Gröger, H. (2019). Detection and fragmentation of doubly charged peptide ions in MALDI-Q-TOF-MS by ion mobility spectrometry for improved protein identification. Analytical and bioanalytical chemistry 411, 1-11.
Sproß, J., Muck, A., & Gröger, H., 2019. Detection and fragmentation of doubly charged peptide ions in MALDI-Q-TOF-MS by ion mobility spectrometry for improved protein identification. Analytical and bioanalytical chemistry, 411(24), p 1-11.
J. Sproß, A. Muck, and H. Gröger, “Detection and fragmentation of doubly charged peptide ions in MALDI-Q-TOF-MS by ion mobility spectrometry for improved protein identification.”, Analytical and bioanalytical chemistry, vol. 411, 2019, pp. 1-11.
Sproß, J., Muck, A., Gröger, H.: Detection and fragmentation of doubly charged peptide ions in MALDI-Q-TOF-MS by ion mobility spectrometry for improved protein identification. Analytical and bioanalytical chemistry. 411, 1-11 (2019).
Sproß, Jens, Muck, Alexander, and Gröger, Harald. “Detection and fragmentation of doubly charged peptide ions in MALDI-Q-TOF-MS by ion mobility spectrometry for improved protein identification.”. Analytical and bioanalytical chemistry 411.24 (2019): 1-11.

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