Fourier transform ion cyclotron resonance (FT ICR) mass spectrometry: Theory and simulations

Nikolaev, E. N.; Kostyukevich, Yury; Vladimirov, Gleb

doi:10.1002/mas.21422

Cited by 162 publications

(134 citation statements)

References 110 publications

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“…FTICR-MS has been shown to provide important clues regarding the nontargeted metabolic proiling and functional characterization of novel genes [47,48]. The compilation of the high mass accuracy and the ultra-highresolving power of FTICR-MS is ideal for the resolving of the analytical problems of the complex-mixtured analyses encountered in proteomics [49,50] and petroleomics [50,51]. [52].…”

Section: Recent Applications Of Fourier Transform Infrared Spectroscomentioning

confidence: 99%

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New Spectral Applications of the Fourier Transforms in Medicine, Biological and Biomedical Fields

Armăşelu¹

2017

Fourier Transforms - High-Tech Application and Current Trends

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This chapter reviews some recent spectral applications of the Fourier transform techniques as they are applied in spectroscopy. An overview about Fourier transform spectroscopy (FTS) used like a powerful and sensitive tool in medical, biological, and biomedical analysis is provided. The advanced spectroscopic techniques of FTS, such as Fourier transform visible spectroscopy (FTVS), Fourier transform infrared-atenuated total relectance (FTIR-ATR), Fourier transform infrared-photoacoustic spectroscopy (FTIR-PAS), Fourier transform infrared imaging spectroscopy (FTIR imaging), and their biomedical applications are described. A special atention has been paid to the description of the FTVS method of commercial quantum dots like an innovative and reliable technique used in the ield of nanobiotechnology.

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Section: Recent Applications Of Fourier Transform Infrared Spectroscomentioning

confidence: 99%

“…Electron capture dissociation (ECD) represents a relatively new technique used for the analysis of peptides and proteins and is a method utilized for inducing fragmentation in FTIR-MS [50]. ECD combined with FTIR-MS represents a powerful and useful technique in proteomic studies.…”

Section: Recent Applications Of Fourier Transform Infrared Spectroscomentioning

confidence: 99%

New Spectral Applications of the Fourier Transforms in Medicine, Biological and Biomedical Fields

Armăşelu¹

2017

Fourier Transforms - High-Tech Application and Current Trends

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“…Recent MS technology such as orbitrap [7] and FT-ICR [8] achieves few to sub ppm m/z resolution and we can easily determine the composition formula nowadays.…”

Section: Introductionmentioning

confidence: 99%

Recent Studies on Online Sample Preconcentration Methods inCapillary Electrophoresis Coupled with Mass Spectrometry

Kawai

2017

Chromatography

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This paper reviews recent 5-years application researches using online sample preconcentration (OSP) methods in capillary electrophoresis (CE) coupled with mass spectrometry (MS). CE-MS has excellent analytical features such as high-resolution separation, rapid analysis time, low sample consumption, and small consumption of organic solvents. Recently, low flow-rate interface for electrospray ionization has been developed and zmol-level sensitivity has been achieved. However, application of CE-MS has still been prevented due to small capacity of sample injection volume. OSP methods have been developed to address this issue and up to 5,000-fold sensitivity improvement was obtained so far. Various application has been carried out such as proteomics, metabolomics, and glycomics, and CE-MS attracts much attention as the highest-performance analytical tool for small-volume bioanalysis. Taking account of further progress in CE-MS, smart and practical application of OSP methods will be more important in various analytical fields.

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“…This was used as an orthogonal approach to top-and middle-down analyses with multiple fragmentation techniques including electron capture dissociation (ECD) [10], electron transfer dissociation (ETD) [11], and MALDI-in-source decay (ISD) [12]. All these fragmentation methods were employed on one of two high-resolution MS instruments, a Fourier transform ion cyclotron resonance (FT-ICR) MS [13,14] or an Orbitrap Elite MS. FT-ICR data were further processed by application of a novel phase correction software, Autophaser [15]. We determined heterogeneous combinations of glycosylation on intact form of the proteins with high relevance to the glycan profiling.…”

Section: Introductionmentioning

confidence: 99%

Comprehensive glycosylation profiling of IgG and IgG-fusion proteins by top-down MS with multiple fragmentation techniques

Tran

Barton²,

Feng³

et al. 2016

Journal of Proteomics

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We employed top-and middle-down analyses with multiple fragmentation techniques including electron transfer dissociation (ETD), electron capture dissociation (ECD), and matrix-assisted laser desorption ionization in-source decay (MALDI-ISD) for characterization of a reference monoclonal antibody (mAb) IgG1 and a fusion IgG protein. Fourier transform ion cyclotron resonance (FT-ICR) or high performance liquid chromatography electrospray ionization (HPLC-ESI) on an Orbitrap was employed. These experiments provided a comprehensive view on the protein species; especially for different glycosylation level in these two proteins, which showed good agreement with oligosaccharide profiling. Top-and middle-down MS provided additional information regarding glycosylation sites and different combinational protein species that were not available from oligosaccharide mapping or conventional bottom-up analysis. Finally, incorporating a limited enzymatic digestion by immunoglobulin G-degrading enzyme of Streptococcus pyogene (IdeS) with MALDI-ISD analysis enabled extended sequence coverage of the internal region of protein without pre-fractionation. Biological significance: Oligosaccharide profiling together with top-and middle-down methods enabled: 1) detection of heterogeneous glycosylated protein species and sites in intact IgG1 and fusion proteins with high mass accuracy, 2) estimation of relative abundance levels of protein species in the sample, 3) confirmation of the protein termini structural information, and 4) improved sequence coverage by MALDI-ISD analysis for the internal regions of the proteins without sample pre-fractionation.

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Fourier transform ion cyclotron resonance (FT ICR) mass spectrometry: Theory and simulations

Cited by 162 publications

References 110 publications

New Spectral Applications of the Fourier Transforms in Medicine, Biological and Biomedical Fields

New Spectral Applications of the Fourier Transforms in Medicine, Biological and Biomedical Fields

Recent Studies on Online Sample Preconcentration Methods inCapillary Electrophoresis Coupled with Mass Spectrometry

Comprehensive glycosylation profiling of IgG and IgG-fusion proteins by top-down MS with multiple fragmentation techniques

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