Developments in ion mobility spectrometry–mass spectrometry

Collins, David C.; Lee, M L

doi:10.1007/s00216-001-1195-5

Cited by 150 publications

(89 citation statements)

References 53 publications

(69 reference statements)

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“…Instrument characteristics and the use of a new ion trap controller and software modifications to control the entire instrument are described. Ion mobility (IM) [4,5] has become a very useful technique for analysis of biological ions in the gas phase [6]. IM provides information about ion size and structure [7], as it rapidly separates ions based on collision cross-section, rather than just m/z ratio.…”

mentioning

confidence: 99%

An ion trap-ion mobility-time of flight mass spectrometer with three ion sources for ion/ion reactions

Zhao

Soyk

Schieffer

et al. 2009

J. Am. Soc. Mass Spectrom.

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This instrument combines the capabilities of ion/ion reactions with ion mobility (IM) and time-of-flight (TOF) measurements for conformation studies and top-down analysis of large biomolecules. Ubiquitin ions from either of two electrospray ionization (ESI) sources are stored in a three dimensional (3D) ion trap (IT) and reacted with negative ions from atmospheric sampling glow discharge ionization (ASGDI). The proton transfer reaction products are then separated by IM and analyzed via a TOF mass analyzer. In this way, ubiquitin ϩ7 ions are converted to lower charge states down to ϩ1; the ions in lower charge states tend to be in compact conformations with cross sections down to ϳ880 Å 2 . The duration and magnitude of the ion ejection pulse on the IT exit and the entrance voltage on the IM drift tube can affect the measured distribution of conformers for ubiquitin ϩ7 and ϩ6. Alternatively, protein ions are fragmented by collision-induced dissociation (CID) in the IT, followed by ion/ion reactions to reduce the charge states of the CID product ions, thus simplifying assignment of charge states and fragments using the mobility-resolved tandem mass spectrum. Instrument characteristics and the use of a new ion trap controller and software modifications to control the entire instrument are described. Ion mobility (IM) [4,5] has become a very useful technique for analysis of biological ions in the gas phase [6]. IM provides information about ion size and structure [7], as it rapidly separates ions based on collision cross-section, rather than just m/z ratio. The use of IM to disperse a mixture of ions in time before analysis via a time-of-flight (TOF) MS, i.e., nested drift (flight) time measurements, is an important recent advance. These experiments were pioneered by Clemmer and coworkers in the mid-1990s [8], and have now been used by several other groups [9 -13]. The recent Synapt ESI-IMS-MS by Waters Corp. provides a commercially available instrument for gas-phase ion conformation studies by IM using a novel traveling wave approach [9].In a series of instrumental designs, the Clemmer group has made various modifications to the initial ESI-IM-TOF, including the insertion of a collision cell between the IM drift tube and the TOF for mobility labeling experiments [14,15], and the addition of an IT before the mobility drift tube to improve the duty cycle from the continuous ESI source [16,17]. One publication demonstrated MS/MS capabilities with an ion trap before IM-TOF [18], but the entire instrument was not under computer control. Therefore, only relatively simple experiments were possible.IM has been used to analyze the products of ionmolecule reactions [19], including proton transfer [20,21], H/D exchange [22], and solvation [23][24][25][26]. In these studies, the desired reactions take place either in the atmospheric pressure ion source interface region or in the drift tube itself. Thus, only short reaction times and certain reagent ions can be used. In addition, performing reactions in the IM cell can make spe...

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confidence: 99%

An ion trap-ion mobility-time of flight mass spectrometer with three ion sources for ion/ion reactions

Zhao

Soyk

Schieffer

et al. 2009

J. Am. Soc. Mass Spectrom.

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“…The coupling of IM to mass spectrometry (IM-MS) has been used for the analysis of a large variety of samples including explosives, drug molecules, biomolecules, etc. [16,17]. Furthermore, IM-MS has been employed successfully for the analysis of structural isomers [18].…”

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Direct tissue analysis of phospholipids in rat brain using MALDI-TOFMS and MALDI-ion mobility-TOFMS

Jackson

Wang

Woods

et al. 2005

J. Am. Soc. Mass Spectrom.

152

144

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After water, lipids are the most common biomolecules found in the brain (12%). A brief perusal of the physiology, anatomy, and pathophysiology of the brain illustrates the importance of lipids. Recent advances in mass spectrometry have allowed the direct probing of tissues. However, most studies have focused on proteins. In the present work, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) and MALDI-ion mobility (IM)-TOFMS were employed for direct analysis of phospholipids in rat brain tissue. Molecular ions (MH ϩ ) corresponding to phosphatidylcholines, phosphatidylethanolamines, and sphingomyelin, were recorded. When studying pharmacology, we learn that many therapeutic compounds are stored in the body's adipose tissue. MALDI-TOFMS and MALDI-IM-TOFMS were thus used to analyze rat brain tissue with chlorisondamine added directly onto the tissue slice. With both techniques, noncovalent complexes between the tissue phospholipids and chlorisondamine were detected. In addition, MALDI-IM-TOFMS of noncovalent complexes between phospholipids and chlorisondamine displayed a mobility between that of an isobaric lipid and peptide. (J Am Soc Mass Spectrom 2005, 16, 133-138)

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“…Ion mobility spectrometry (IMS) is a measurement technique where ionized analytes are separated based their mobilities under electric field in flow of neutral gas or air under ambient pressure conditions [3]. A combining IMS together with MS provides a very promising hyphenated technique, especially since mass spectrometry characterizes the ions by mass to charge ratio and therefore allows identification of the ion clusters, which were broken apart in the APi [4].…”

Section: Introductionmentioning

confidence: 99%

Cluster measurements at CLOUD using a high resolution ion mobility spectrometer-mass spectrometer combination

Adamov

Junninen

Duplissy

et al. 2013

AIP Conference Proceedings

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Articles you may be interested inCombining high mass resolution and velocity imaging in a time-of-flight ion spectrometer using pulsed fields and an electrostatic lens Rev. Sci. Instrum. 78, 083104 (2007) Abstract. Mass spectrometry is powerful tool for environmental and atmospheric chemistry analysis. Modern mass spectrometers demonstrate low detection limits, high sensitivity, and high resolving power. However, such high performance is not always enough to identify ambient ion clusters due to the clusters braking at the atmospheric pressure-to-vacuum interface of mass spectrometer. This study presents a high resolution ion mobility spectrometer -time-of-flight mass spectrometer (IMS-TOF) in the CLOUD experiment. This combination of orthogonal analytical techniques allows obtaining structural information in addition to mass-to-charge separation.

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Developments in ion mobility spectrometry–mass spectrometry

Cited by 150 publications

References 53 publications

An ion trap-ion mobility-time of flight mass spectrometer with three ion sources for ion/ion reactions

An ion trap-ion mobility-time of flight mass spectrometer with three ion sources for ion/ion reactions

Direct tissue analysis of phospholipids in rat brain using MALDI-TOFMS and MALDI-ion mobility-TOFMS

Cluster measurements at CLOUD using a high resolution ion mobility spectrometer-mass spectrometer combination

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