A review on the application of high‐field asymmetric waveform ion mobility spectrometry (FAIMS) in drug discovery

Hatsis, Panos; Kapron, James T.

doi:10.1002/rcm.3416

Cited by 50 publications

(33 citation statements)

References 12 publications

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“…A later type of ion mobility spectrometry, field asymmetric ion mobility spectrometry (FAIMS) [4,[16][17][18][19][20][21] or differential ion mobility spectrometry (DMS) [18,19,[22][23][24][25][26], has been developed that depends on this non-linearity. The mobility coefficient at a given temperature depends on the density normalized electric field strength and this dependence may be represented by Eq.…”

Section: Introductionmentioning

confidence: 99%

A determination of the effective temperatures for the dissociation of the proton bound dimer of dimethyl methylphosphonate in a planar differential mobility spectrometer

Eiceman

Stone

2010

Int. J. Ion Mobil. Spec.

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The dissociation of the proton bound dimer of dimethyl methylphosphonate to the protonated and neutral molecule has been studied in a planar differential mobility spectrometer. The internal energy of the ions is the sum of the thermal component and the electric field component and results in an effective temperature, T eff , that is significantly greater than that of the ambient atmosphere temperature, T. The measured rate constant for dissociation, which rises exponentially with field strength, together with activation energy and pre-exponential factor previously determined under thermal conditions, allow the calculation of T eff as a function of electric field strength. T eff is a linear function of electric field intensity at constant T over the range of T from 60°C to 140°C. The efficiency of the available collision energy in causing dissociation decreases with increasing T, from 52% at 60°C to 40% at 140°C.

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Section: Introductionmentioning

confidence: 99%

A determination of the effective temperatures for the dissociation of the proton bound dimer of dimethyl methylphosphonate in a planar differential mobility spectrometer

Eiceman

Stone

2010

Int. J. Ion Mobil. Spec.

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“…IM adds a separation dimension (reported as drift time) to mass spectrometry, which is comparable to the retention time of liquid chromatography (LC) and gas chromatography (GC) hyphenated MS methods. Since its inception in 1980s, ion mobility has evolved rapidly, with the emergence of alternatives to the classic drift tubes: field asymmetric waveform ion mobility spectrometry (FAIMS) and, these days, the traveling wave (T-wave) [41,42]. Initially, IM was used to differentiate conformers in the gas phase, but more recently IMMS has been applied to protein conformer differentiation, top-down protein sequencing, noncovalent protein complexes, isobaric compound identification, and imaging by mass spectrometry [43][44][45][46].…”

mentioning

confidence: 99%

On-tissue protein identification and imaging by MALDI-Ion mobility mass spectrometry

Stauber

MacAleese

Franck

et al. 2010

J. Am. Soc. Mass Spectrom.

184

160

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MALDI imaging mass spectrometry (MALDI-IMS) has become a powerful tool for the detection and localization of drugs, proteins, and lipids on-tissue. Nevertheless, this approach can only perform identification of low mass molecules as lipids, pharmaceuticals, and peptides. In this article, a combination of approaches for the detection and imaging of proteins and their identification directly on-tissue is described after tryptic digestion. Enzymatic digestion protocols for different kinds of tissues-formalin fixed paraffin embedded (FFPE) and frozen tissues-are combined with MALDI-ion mobility mass spectrometry (IM-MS). This combination enables localization and identification of proteins via their related digested peptides. In a number of cases, ion mobility separates isobaric ions that cannot be identified by conventional MALDI time-of-flight (TOF) mass spectrometry. The amount of detected peaks per measurement increases (versus conventional MALDI-TOF), which enables mass and time selected ion images and the identification of separated ions. These experiments demonstrate the feasibility of direct proteins identification by ion-mobility-TOF IMS from tissue. The tissue digestion combined with MALDI-IM-TOF-IMS approach allows a proteomics "bottom-up" strategy with different kinds of tissue samples, especially FFPE tissues conserved for a long time in hospital sample banks. The combination of IM with IMS marks the development of IMS approaches as real proteomic tools, which brings new perspectives to biological studies. (J Am Soc Mass Spectrom 2010, 21, 338 -347)

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“…The principle of this additional separation technique is that the ion mobility at high electric fields can differ according to the shape of the ions. Therefore, FAIMS can separate isomeric or isobaric analytes that the LC and ordinary MS cannot (Hatsis and Kapron 2008). On a model acyl-glucuronide of ifetroban Xia et al have demonstrated the use of FAIMS for locating the place where the acyl glucuronide is being fragmented to its parent inside the mass spectrometer ).…”

Section: Mass Spectrometry Operation Modes For Glucuronide Detectionmentioning

confidence: 99%

Quantification of Glucuronide Metabolites in Biological Matrices by LC-MS/MS

Trontelj¹

2012

Tandem Mass Spectrometry - Applications and Principles

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A review on the application of high‐field asymmetric waveform ion mobility spectrometry (FAIMS) in drug discovery

Cited by 50 publications

References 12 publications

A determination of the effective temperatures for the dissociation of the proton bound dimer of dimethyl methylphosphonate in a planar differential mobility spectrometer

A determination of the effective temperatures for the dissociation of the proton bound dimer of dimethyl methylphosphonate in a planar differential mobility spectrometer

On-tissue protein identification and imaging by MALDI-Ion mobility mass spectrometry

Quantification of Glucuronide Metabolites in Biological Matrices by LC-MS/MS

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