Preliminary investigation of ion mobility spectrometry after capillary electrophoretic introduction

Hallen, R.W.; Shumate, Christopher B.; Siems, William F.; Tsuda, Toshitaka; Hill, Herbert H.

doi:10.1016/s0021-9673(01)84291-6

Cited by 43 publications

(21 citation statements)

References 10 publications

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“…However, although TBA and TPA ion mobilities were more stable than those of DTBP in the presence of contaminants, their reduced mobilities are not well established, and more investigations are required to determine accurate and precise mobilities of these ions to replace DTBP as the instrument standard of choice in IMS. The reduced mobility values reported for TBA ions ranged from 1.19 to 1.40 cm 2 V −1 s −1 with an average value of 1.30 cm 2 V −1 s −1 ;25,37,47,52–53 this variability may be due to inaccurate measurement of instrumental parameters.…”

Section: Resultsmentioning

confidence: 97%

Chemical standards in ion mobility spectrometry

Fernandez‐Maestre

Harden

Ewing

et al. 2010

Analyst

103

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In ion mobility spectrometry (IMS), reduced mobility values (K0) are used as a qualitative measure of gas phase ions, and are reported in the literature as absolute values. Unfortunately, these values do not always match those collected in the field. One reason for this discrepancy is that the buffer gas may be contaminated with moisture or other volatile compounds. In this study, the effect of moisture and organic contaminants in the buffer gas on the mobility of IMS standards and analytes was investigated for the first time using IMS directly coupled to mass spectrometry. 2,4-dimethylpyridine, 2,6-di-tert-butyl pyridine (DTBP), and tetrabutylammonium, tetrapropylammonium, tetraethylammonium, and tetramethylammonium chlorides were used as chemical standards. In general, the mobility of IMS standard product ions was not affected by small amounts of contamination while the mobilities of many analytes were affected. In the presence of contaminants in the buffer gas, the mobility of analyte ions is often decreased by forming ionmolecule clusters with the contaminant. To ensure the measurement of accurate reduced mobility values, two IMS standards are required: an instrument and a mobility standard. An instrument standard is not affected by contaminants in the buffer gas, and provides an accurate measurement of the instrumental parameters, such as voltage, drift length, pressure, and temperature. The mobility standard behaves like an analyte ion in that the compound's mobility is affected by low levels of contamination in the buffer gas. Prudent use of both of these standards can lead to improved measurement of accurate reduced mobility values.

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Section: Resultsmentioning

confidence: 97%

Chemical standards in ion mobility spectrometry

Fernandez‐Maestre

Harden

Ewing

et al. 2010

Analyst

103

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“…Despite these commonalities, only a few cases of CE and DTIMS-MS as complementary or comparative techniques exist (104, 105). The first attempt to couple CE and DTIMS was performed by the Hill group in 1989 (106) with their newly developed ESI source for the IMS instrument (107). However, spray instability made this coupling difficult and hindered its initial application.…”

Section: Capillary Electrophoresis–drift Tube Ion Mobility Spectrometmentioning

confidence: 99%

Coupling Front-End Separations, Ion Mobility Spectrometry, and Mass Spectrometry For Enhanced Multidimensional Biological and Environmental Analyses

Zheng

Wojcik

Zhang

et al. 2017

Annual Rev. Anal. Chem.

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Ion mobility spectrometry (IMS) is a widely used analytical technique for rapid molecular separations in the gas phase. Though IMS alone is useful, its coupling with mass spectrometry (MS) and front-end separations is extremely beneficial for increasing measurement sensitivity, peak capacity of complex mixtures, and the scope of molecular information available from biological and environmental sample analyses. In fact, multiple disease screening and environmental evaluations have illustrated that the IMS-based multidimensional separations extract information that cannot be acquired with each technique individually. This review highlights three-dimensional separations using IMS-MS in conjunction with a range of front-end techniques, such as gas chromatography, supercritical fluid chromatography, liquid chromatography, solid-phase extractions, capillary electrophoresis, field asymmetric ion mobility spectrometry, and microfluidic devices. The origination, current state, various applications, and future capabilities of these multidimensional approaches are described in detail to provide insight into their uses and benefits.

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“…The use of IMS therefore brings additional selectivity by electrophoretically resolving and simplifying ion populations on the millisecond timescale 33. The evolution of IMS has resulted in a wide range of hyphenated IMS applications, including coupling with gas chromatography (GC/IMS) for the analysis of explosives,34 liquid chromatography (LC/IMS) for pharmaceutical analysis,35 capillary electrophoresis (CE/IMS),36 and mass spectrometry (IMS/MS) 37–39. In more complex hybrid systems, IMS has been combined with quadrupole time‐of‐flight mass spectrometry (QToF‐MS) to form nested, three‐dimensional (IMS drift time, m/z , signal intensity) data sets.…”

mentioning

confidence: 99%

Analysis of tryptic peptides using desorption electrospray ionisation combined with ion mobility spectrometry/mass spectrometry

Kaur-Atwal

Weston

Green

et al. 2007

Rapid Comm Mass Spectrometry

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A novel method is reported for rapid protein identification by the analysis of tryptic peptides using desorption electrospray ionisation (DESI) coupled with hyphenated ion mobility spectrometry and quadrupole time-of-flight mass spectrometry (IMS/Q-ToF-MS). Confident protein identification is demonstrated for the analysis of tryptically digested bovine serum albumin (BSA), with no sample pre-treatment or clean-up. Electrophoretic ion mobility separation of ions generated by DESI allowed examination of charge-state and mobility distributions for tryptic peptide mixtures. Selective interrogation of singly charged ions allowed isobaric peptide responses to be distinguished, along with a reduction in spectral noise. The mobility-selected singly charged peptide responses were presented as a pseudo-peptide mass fingerprint (p-PMF) for protein database searching. Comparative data are shown for electrospray ionisation (ESI) of the BSA digest, without sample clean-up, from which confident protein identification could not be made. Implications for the robustness of the DESI method, together with potential insights into mechanisms for DESI of proteolytic digests, are discussed.

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Preliminary investigation of ion mobility spectrometry after capillary electrophoretic introduction

Cited by 43 publications

References 10 publications

Chemical standards in ion mobility spectrometry

Chemical standards in ion mobility spectrometry

Coupling Front-End Separations, Ion Mobility Spectrometry, and Mass Spectrometry For Enhanced Multidimensional Biological and Environmental Analyses

Analysis of tryptic peptides using desorption electrospray ionisation combined with ion mobility spectrometry/mass spectrometry

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