Traveling Wave Ion Mobility Mass Spectrometry

Proteomic and Biopharmaceutical Applications

  • Fig. 1: Schematic diagram of the Synapt G2-S hybrid quadrupole - ion mobility - orthogonal acceleration time-of-flight mass spectrometer.Fig. 1: Schematic diagram of the Synapt G2-S hybrid quadrupole - ion mobility - orthogonal acceleration time-of-flight mass spectrometer.
  • Fig. 1: Schematic diagram of the Synapt G2-S hybrid quadrupole - ion mobility - orthogonal acceleration time-of-flight mass spectrometer.
  • Fig. 2: Intact tandem MS ETD spectrum obtained melittin. Shown inset is the mobility separation of the overlapping c8+ and z122+ product ions and the corresponding mass spectra.
  • Fig. 3: DIA identification and sequence annotation of VTEVVVK from clusterin obtained from rat exosomes in LC-DIA-MS (top) and LC-DIA-IM-MS mode (bottom) [4]. Product ion color legend: y (red), b (blue), green (neutral loss of H2O or NH2), co-eluting (brown) and non-identified (grey).
  • Fig. 4: CID (top), ETD (middle) and ETD IM-MS (bottom) product ion spectra synthetic EAISPPDAA (*HexNAcS) AAPLR from erythropoietin

Mass spectrometry (MS) has evolved into an indispensible analytical technique for the structural determination of samples encountered in chemical, biopharmaceutical and proteomics type research. These research areas have led the demand for alternative mass-analyzer types and the combination of ion mobility (IM) with MS. Ion mobility spectrometry provides a specific probe for investigating both the structural and conformational properties of gas-phase ions. Since the mobility of ions is governed by size, shape and charge, the combination of IM-MS provides both mass-to-charge and shape-to-charge information in a single experiment. Traditionally, IM has been used to detect explosives and chemical warfare agents, which pose a threat to homeland security. However, IM-MS is now being used as a research tool as well for the analysis of very complex mixtures often encountered in both chemical and biological samples [1].

IM can be incorporated into liquid chromatography (LC)-oa-ToF systems providing elution time, mobility drift time and m/z information of the ionic species being sampled. Ionic species that exhibit the same elution time in the LC domain maybe distinguished in the mobility domain, since they can be temporally separated and independently detected. The commercial implementation of IM into an oa-ToF mass spectro­meter involved the use and exploration of traveling wave ion guides for mobility based separations [2]. The analytical use of these devices for chemical, biopharmaceutical and proteomics applications reaches however beyond IM separation as will be demonstrated in this publication.

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