skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

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

Abstract

Ion mobility spectrometry (IMS) is a widely used analytical technique for rapid molecular separations in the gas phase. IMS alone is useful, but its coupling with mass spectrometry (MS) and front-end separations has been extremely beneficial for increasing measurement sensitivity, peak capacity of complex mixtures, and the scope of molecular information in biological and environmental sample analyses. Multiple studies in disease screening and environmental evaluations have even shown these IMS-based multidimensional separations extract information not possible with each technique individually. This review highlights 3-dimensional separations using IMS-MS in conjunction with a range of front-end techniques, such as gas chromatography (GC), supercritical fluid chromatography (SFC), liquid chromatography (LC), solid phase extractions (SPE), capillary electrophoresis (CE), field asymmetric ion mobility spectrometry (FAIMS), and microfluidic devices. The origination, current state, various applications, and future capabilities for these multidimensional approaches are described to provide insight into the utility and potential of each technique.

Authors:
 [1];  [1];  [2];  [1];  [1];  [1];  [1];  [1];  [1];  [1]
  1. Earth and Biological Sciences Directorate, Pacific Northwest National Laboratory, Richland, Washington 99352,
  2. Skaggs School of Pharmacy and Pharmaceutical Sciences, Anschutz Medical Campus, University of Colorado, Denver, Colorado 80045
Publication Date:
Research Org.:
Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
Sponsoring Org.:
USDOE
OSTI Identifier:
1373001
Report Number(s):
PNNL-SA-121198
Journal ID: ISSN 1936-1327; 48680; 48199; 49531; KP1601010; 453040220; 400412000; WN9030198
DOE Contract Number:
AC05-76RL01830
Resource Type:
Journal Article
Resource Relation:
Journal Name: Annual Review of Analytical Chemistry; Journal Volume: 10; Journal Issue: 1
Country of Publication:
United States
Language:
English
Subject:
ion mobility; Spectrometry; Mass spectrometry; Environmental Molecular Sciences Laboratory

Citation Formats

Zheng, Xueyun, Wojcik, Roza, Zhang, Xing, Ibrahim, Yehia M., Burnum-Johnson, Kristin E., Orton, Daniel J., Monroe, Matthew E., Moore, Ronald J., Smith, Richard D., and Baker, Erin S. Coupling Front-End Separations, Ion Mobility Spectrometry, and Mass Spectrometry For Enhanced Multidimensional Biological and Environmental Analyses. United States: N. p., 2017. Web. doi:10.1146/annurev-anchem-061516-045212.
Zheng, Xueyun, Wojcik, Roza, Zhang, Xing, Ibrahim, Yehia M., Burnum-Johnson, Kristin E., Orton, Daniel J., Monroe, Matthew E., Moore, Ronald J., Smith, Richard D., & Baker, Erin S. Coupling Front-End Separations, Ion Mobility Spectrometry, and Mass Spectrometry For Enhanced Multidimensional Biological and Environmental Analyses. United States. doi:10.1146/annurev-anchem-061516-045212.
Zheng, Xueyun, Wojcik, Roza, Zhang, Xing, Ibrahim, Yehia M., Burnum-Johnson, Kristin E., Orton, Daniel J., Monroe, Matthew E., Moore, Ronald J., Smith, Richard D., and Baker, Erin S. Mon . "Coupling Front-End Separations, Ion Mobility Spectrometry, and Mass Spectrometry For Enhanced Multidimensional Biological and Environmental Analyses". United States. doi:10.1146/annurev-anchem-061516-045212.
@article{osti_1373001,
title = {Coupling Front-End Separations, Ion Mobility Spectrometry, and Mass Spectrometry For Enhanced Multidimensional Biological and Environmental Analyses},
author = {Zheng, Xueyun and Wojcik, Roza and Zhang, Xing and Ibrahim, Yehia M. and Burnum-Johnson, Kristin E. and Orton, Daniel J. and Monroe, Matthew E. and Moore, Ronald J. and Smith, Richard D. and Baker, Erin S.},
abstractNote = {Ion mobility spectrometry (IMS) is a widely used analytical technique for rapid molecular separations in the gas phase. IMS alone is useful, but its coupling with mass spectrometry (MS) and front-end separations has been extremely beneficial for increasing measurement sensitivity, peak capacity of complex mixtures, and the scope of molecular information in biological and environmental sample analyses. Multiple studies in disease screening and environmental evaluations have even shown these IMS-based multidimensional separations extract information not possible with each technique individually. This review highlights 3-dimensional separations using IMS-MS in conjunction with a range of front-end techniques, such as gas chromatography (GC), supercritical fluid chromatography (SFC), liquid chromatography (LC), solid phase extractions (SPE), capillary electrophoresis (CE), field asymmetric ion mobility spectrometry (FAIMS), and microfluidic devices. The origination, current state, various applications, and future capabilities for these multidimensional approaches are described to provide insight into the utility and potential of each technique.},
doi = {10.1146/annurev-anchem-061516-045212},
journal = {Annual Review of Analytical Chemistry},
number = 1,
volume = 10,
place = {United States},
year = {Mon Jun 12 00:00:00 EDT 2017},
month = {Mon Jun 12 00:00:00 EDT 2017}
}
  • We report the first evaluation of a platform coupling a high speed field asymmetric ion mobility spectrometry microchip (µFAIMS) with drift tube ion mobility and mass spectrometry (IMS-MS). The µFAIMS/IMS-MS platform was used to analyze biological samples and simultaneously acquire multidimensional information of detected features from the measured FAIMS compensation fields and IMS drift times, while also obtaining accurate ion masses. These separations thereby increase the overall separation power, resulting increased information content, and provide more complete characterization of more complex samples. The separation conditions were optimized for sensitivity and resolving power by the selection of gas compositions and pressuresmore » in the FAIMS and IMS separation stages. The resulting performance provided three dimensional separations, benefitting both broad complex mixture studies and targeted analyses by e.g. improving isomeric separations and allowing detection of species obscured by “chemical noise” and other interfering peaks.« less
  • Glycomics has become an increasingly important field of research since glycans play critical roles in biology processes ranging from molecular recognition and signaling to cellular communication. Glycans often conjugate with other biomolecules such as proteins and lipids, and alter their properties and functions, so understanding the effect glycans have on cellular systems is essential. However the analysis of glycans is extremely difficult due to their complexity and structural diversity (i.e., the number and identity of monomer units, and configuration of their glycosidic linkages and connectivities). In this work, we coupled ion mobility spectrometry with mass spectrometry (IMS-MS) to characterize glycanmore » standards and biologically important isomers of synthetic αGal-containing O-glycans including glycotopes of the protozoan parasite Trypanosoma cruzi, which is the causative agent of Chagas disease. IMS-MS results showed significant differences for the glycan structural isomers when analyzed in positive and negative polarity and complexed with different metal cations. These results suggest specific metal ions or ion polarities could be used to target and baseline separate glycan isomers of interest with IMS-MS.« less
  • There is significant interest in characterization of the human plasma proteome due to its potential for providing biomarkers applicable to clinical diagnosis and treatment and for gaining a better understanding of human diseases. We describe here a strategy for comparative proteome analyses of human plasma, which is applicable to biomarker identifications for various disease states. Multidimensional liquid chromatography-mass spectrometry has been applied to make comparative proteome analyses of plasma samples from an individual prior to and 9 h after lipopolysaccharide (LPS) administration. Peptide peak areas and the number of peptide identifications for each protein were used to evaluate the reproducibilitymore » of LC-MS/MS and to compare relative changes in protein concentration between the samples following LPS treatment. A total of 1563 distinct plasma proteins were confidently identified with 26 proteins observed to be significantly increased in concentration following LPS administration, including several known inflammatory response or acute-phase mediators, and thus constitute potential biomarkers for inflammatory response.« less
  • There is significant interest in characterization of the human plasma proteome due to its potential for providing biomarkers applicable to clinical diagnosis and treatment and for gaining a better understanding of human diseases. We describe here a strategy for comparative proteome analyses of human plasma, which is applicable to biomarker identifications for various disease states. Multidimensional liquid chromatography-mass spectrometry has been applied to make comparative proteome analyses of plasma samples from an individual prior to and 9 h after lipopolysaccharide (LPS) administration. Peptide peak areas and the number of peptide identifications for each protein were used to evaluate the reproducibilitymore » of LC-MS/MS and to compare relative changes in protein concentration between the samples following LPS treatment. A total of 804 distinct plasma proteins (not including immunoglobulins) were confidently identified with 32 proteins observed to be significantly increased in concentration following LPS administration, including several known inflammatory response or acute-phase mediators such as C-reactive protein, serum amyloid A and A2, LPS-binding protein, LPS-responsive and beige-like anchor protein, hepatocyte growth factor activator and von Willebrand factor, and thus constituting potential biomarkers for inflammatory response.« less
  • Understanding the biological mechanisms related to lipids and glycolipids is challenging due to the vast number of possible isomers. Mass spectrometry (MS) measurements are currently the dominant approach for studying and providing detailed information on lipid and glycolipid structures. However, difficulties in distinguishing many structural isomers (e.g. distinct acyl chain positions, double bond locations, as well as glycan isomers) inhibit the understanding of their biological roles. Here we utilized ultra-high resolution ion mobility spectrometry (IMS) separations based upon the use of traveling waves in a serpentine long path length multi-pass Structures for Lossless Manipulations (SLIM) to enhance isomer resolution. Themore » multi-pass arrangement allowed separations ranging from ~16 m (1 pass) to ~470 m (32 passes) to be investigated for the distinction of lipids and glycolipids with extremely small structural differences. Lastly, these ultra-high resolution SLIM IMS-MS analyses provide a foundation for exploring and better understanding isomer specific biological and disease processes.« less