Analytical and Bioanalytical Chemistry

, Volume 405, Issue 1, pp 51–61 | Cite as

Towards analytically useful two-dimensional Fourier transform ion cyclotron resonance mass spectrometry

  • Maria A. van Agthoven
  • Marc-André Delsuc
  • Geoffrey Bodenhausen
  • Christian Rolando
Review

Abstract

Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry (MS) achieves high resolution and mass accuracy, allowing the identification of the raw chemical formulae of ions in complex samples. Using ion isolation and fragmentation (MS/MS), we can obtain more structural information, but MS/MS is time- and sample-consuming because each ion must be isolated before fragmentation. In 1987, Pfändler et al. proposed an experiment for 2D FT-ICR MS in order to fragment ions without isolating them and to visualize the fragmentations of complex samples in a single 2D mass spectrum, like 2D NMR spectroscopy. Because of limitations of electronics and computers, few studies have been conducted with this technique. The improvement of modern computers and the use of digital electronics for FT-ICR hardware now make it possible to acquire 2D mass spectra over a broad mass range. The original experiments used in-cell collision-induced dissociation, which caused a loss of resolution. Gas-free fragmentation modes such as infrared multiphoton dissociation and electron capture dissociation allow one to measure high-resolution 2D mass spectra. Consequently, there is renewed interest to develop 2D FT-ICR MS into an efficient analytical method. Improvements introduced in 2D NMR spectroscopy can also be transposed to 2D FT-ICR MS. We describe the history of 2D FT-ICR MS, introduce recent improvements, and present analytical applications to map the fragmentation of peptides. Finally, we provide a glossary which defines a few keywords for the 2D FT-ICR MS field.

Keywords

Mass spectrometry Fourier transform ion cyclotron resonance Two-dimensional FT-ICR 

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Copyright information

© Springer-Verlag Berlin Heidelberg 2012

Authors and Affiliations

  • Maria A. van Agthoven
    • 1
  • Marc-André Delsuc
    • 2
  • Geoffrey Bodenhausen
    • 3
  • Christian Rolando
    • 1
  1. 1.Miniaturisation pour la Synthèse l’Analyse et la Protéomique, USR CNRS 3290, Institut Michel-Eugène Chevreul, FR CNRS 2638 and Protéomique, Modifications Post-Traductionnelles et Glycobiologie, IFR 147 Université de Lille 1, Sciences et TechnologieVilleneuve d’Ascq CedexFrance
  2. 2.U 596 and UMR CNRS 7104, Institut de Génétique et de Biologie Moléculaire et Cellulaire, INSERMUniversité de StrasbourgIllkirch-GraffenstadenFrance
  3. 3.UMR 7203, Département de ChimieÉcole Normale SupérieureParis Cedex 05France

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