M. A. Van Agthoven, M. A. Delsuc, G. Bodenhausen, C. Rolando
Anal. Bioanal. Chem. 405 51-61 (2013). DOI

Travail réalisé sur le site de l’Université de Lille 1, Sciences et Technologies.

Abstract

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Fourier Transform Ion Cyclotron Resonance Mass Spectrometry (FT-ICR 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 two-dimensional FT-ICR MS in order to fragment ions without isolating them and to visualize the fragmentations of complex samples in a single two-dimensional mass spectrum, like 2D NMR. Because of limitations of electronics and computers, few studies have been carried out 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. Original experiments used in-cell CID that caused a loss of resolution. Gas-free fragmentation modes like IRMPD and ECD 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 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 introduce a glossary which defines a few key words for the 2D FT-ICR MS field.