Field Asymmetric Waveform Ion Mobility Spectrometry Analysis of Proteins and Peptides: A Review

Brown, Lauren J.; Creaser, Colin S.

doi:10.2174/1573411011309020005

Cited by 5 publications

(4 citation statements)

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“…However, ESI-FAIMS-MS allows for the separation of ions based upon compound-dependent differences in high and low field mobility as a result of charge state [33,36,41]. FAIMS separation may therefore be used to suppress or enhance the transmission of singly or multiply charged ions selectively.…”

Section: + 2na -H]mentioning

confidence: 99%

Analysis of Supramolecular Complexes of 3-Methylxanthine with Field Asymmetric Waveform Ion Mobility Spectrometry Combined with Mass Spectrometry

Arthur

Eiceman

Reynolds

et al. 2016

J. Am. Soc. Mass Spectrom.

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Abstract. Miniaturised field asymmetric waveform ion mobility spectrometry (FAIMS), combined with mass spectrometry (MS), has been applied to the study of selfassembling, noncovalent supramolecular complexes of 3-methylxanthine (3-MX) in the gas phase. 3-MX forms stable tetrameric complexes around an alkali metal (Na + , K + ) or ammonium cation, to generate a diverse array of complexes with single and multiple charge states. Complexes of (3-MX) n observed include: singly charged complexes where n = 1-8 and 12 and doubly charged complexes where n = 12-24. The most intense ions are those associated with multiples of tetrameric units, where n = 4, 8, 12, 16, 20, 24. The effect of dispersion field on the ion intensities of the self-assembled complexes indicates some fragmentation of higher order complexes within the FAIMS electrodes (in-FAIMS dissociation), as well as in-source collision induced dissociation within the mass spectrometer. FAIMS-MS enables charge state separation of supramolecular complexes of 3-MX and is shown to be capable of separating species with overlapping mass-to-charge ratios. FAIMS selected transmission also results in an improvement in signal-to-noise ratio for low intensity complexes and enables the visualization of species undetectable without FAIMS.

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Section: + 2na -H]mentioning

confidence: 99%

Analysis of Supramolecular Complexes of 3-Methylxanthine with Field Asymmetric Waveform Ion Mobility Spectrometry Combined with Mass Spectrometry

Arthur

Eiceman

Reynolds

et al. 2016

J. Am. Soc. Mass Spectrom.

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“… 29 However, as the desire for IMS measurements of metabolites and xenobiotics continues to grow, so does the need for high quality collision cross section (CCS) values to evaluate the small molecule structures and better develop experimental and theoretical methods. 30 Currently, many IMS techniques are available for analyzing small molecules such as drift tube IMS (DTIMS), 31 – 34 traveling wave IMS (TWIMS), 35 trapped IMS (TIMS), 36 overtone IMS (OIMS), 37 , 38 differential IMS (DIMS), 39 field asymmetric IMS (FAIMS), 40 – 42 and transversal modulation IMS (TM-IMS). 43 DTIMS, however, has a distinct advantage over many of these techniques since its CCS values are a direct reflection of the 3-dimensional size of the molecules and can be performed without calibration.…”

Section: Introductionmentioning

confidence: 99%

A structural examination and collision cross section database for over 500 metabolites and xenobiotics using drift tube ion mobility spectrometry

et al. 2017

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“…For the vast majority of applications, the buffer gas is inert, but there are a few applications where a reactive buffer gas is also desired. Different variations of the application of electric field and stationary state of the buffer gas have given rise to multiple IMS-based platforms such as drift tube IMS (DTIMS), traveling wave IMS (TWIMS), trapped IMS (TIMS), overtone IMS (OIMS), , differential IMS (DIMS), field asymmetric IMS (FAIMS), − and transversal modulation IMS (TM-IMS) . In the classical DTIMS, ions travel through the drift tube under the influence of a weak electric field while colliding with a stationary buffer gas.…”

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confidence: 99%

Development of an Ion Mobility Spectrometry-Orbitrap Mass Spectrometer Platform

et al. 2016

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Complex samples benefit from multidimensional measurements where higher resolution enables more complete characterization of biological and environmental systems. To address this challenge, we developed a drift tube-based ion mobility spectrometry-Orbitrap mass spectrometer (IMS-Orbitrap MS) platform. To circumvent the time scale disparity between the fast IMS separation and the much slower Orbitrap MS acquisition, we utilized a dual gate and pseudorandom sequences to multiplex the injection of ions and allow operation in signal averaging (SA), single multiplexing (SM), and double multiplexing (DM) IMS modes to optimize the signal-to-noise ratio of the measurements. For the SM measurements, a previously developed algorithm was used to reconstruct the IMS data. A new algorithm was developed for the DM analyses involving a two-step process that first recovers the SM data and then decodes the SM data. The algorithm also performs multiple refining procedures to minimize demultiplexing artifacts. The new IMSOrbitrap MS platform was demonstrated by the analysis of proteomic and petroleum samples, where the integration of IMS and high mass resolution proved essential for accurate assignment of molecular formulas.

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Field Asymmetric Waveform Ion Mobility Spectrometry Analysis of Proteins and Peptides: A Review

Cited by 5 publications

References 0 publications

Analysis of Supramolecular Complexes of 3-Methylxanthine with Field Asymmetric Waveform Ion Mobility Spectrometry Combined with Mass Spectrometry

Analysis of Supramolecular Complexes of 3-Methylxanthine with Field Asymmetric Waveform Ion Mobility Spectrometry Combined with Mass Spectrometry

A structural examination and collision cross section database for over 500 metabolites and xenobiotics using drift tube ion mobility spectrometry

Development of an Ion Mobility Spectrometry-Orbitrap Mass Spectrometer Platform

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