Abstract:The ion mobility spectrometry (IMS) methods are grouped into conventional IMS, based on the absolute ion mobility, and differential or field asymmetric waveform IMS (FAIMS), based on the mobility difference in strong and weak electric fields. A key attraction of FAIMS is substantial orthogonality to mass spectrometry (MS). Although several FAIMS/MS platforms were commercialized, their utility was limited by FAIMS resolving power, typically ∼10 - 20. Recently, gas mixtures comprising up to 75% He has enabled re… Show more
“…Other FAIMS devices have achieved higher resolution by using longer ion residence times [169], higher fields [171,172], or different separation gas [172,173]. However, in most of these cases, the degree of heating of the ions caused by the separation fields increases, and this can cause conformer isomerization.…”
Determining the conformation of biological molecules is key for understanding their function. The recent combination of mass spectrometry, cryogenic ion traps, and laser spectroscopy is providing new methods to interrogate individual conformations of peptides and proteins that have advantages over classical techniques of structure determination. This chapter provides an overview of these new state-of-the-art methods and illustrates several specific applications. After reviewing the fundamentals of ion production, trapping, cooling, and spectroscopic detection, we review how different combinations of these techniques have been implemented in various laboratories around the world. We then focus on applications of cryogenic ion spectroscopy from two specific laboratories to illustrate the potential of this general approach. Finally, we outline ways in which these powerful new techniques could be further improved.
“…Other FAIMS devices have achieved higher resolution by using longer ion residence times [169], higher fields [171,172], or different separation gas [172,173]. However, in most of these cases, the degree of heating of the ions caused by the separation fields increases, and this can cause conformer isomerization.…”
Determining the conformation of biological molecules is key for understanding their function. The recent combination of mass spectrometry, cryogenic ion traps, and laser spectroscopy is providing new methods to interrogate individual conformations of peptides and proteins that have advantages over classical techniques of structure determination. This chapter provides an overview of these new state-of-the-art methods and illustrates several specific applications. After reviewing the fundamentals of ion production, trapping, cooling, and spectroscopic detection, we review how different combinations of these techniques have been implemented in various laboratories around the world. We then focus on applications of cryogenic ion spectroscopy from two specific laboratories to illustrate the potential of this general approach. Finally, we outline ways in which these powerful new techniques could be further improved.
“…An increase in the dispersion field ( E D ) of the DIMS waveform increases the resolution of DIMS separations [21, 22], but also leads to a decrease in ion transmission through the assembly. Because the displacement of an ion is directly proportional to the applied electric field (Equations 1 and 2), the oscillation amplitude of the ion ( Δd ) will increase with increasing electric field strength, effectively constraining the analytical gap between the electrodes [23].…”
Differential ion mobility spectrometry (DIMS) has the ability to separate gas phase ions based on their difference in ion mobility in low and high electric fields. DIMS can be used to separate mixtures of isobaric and isomeric species indistinguishable by mass spectrometry (MS). DIMS can also be used as a filter to improve the signal-to-background of analytes in complex samples. The resolving power of DIMS separations can be improved several ways, including increasing the dispersion field and increasing the amount of helium in the nitrogen carrier gas. It has been previously demonstrated that the addition of helium to the DIMS carrier gas provides improves separations when the dispersion field is the kept constant as helium content is varied. However, helium has a lower breakdown voltage than nitrogen. Therefore, as the percent helium content in the nitrogen carrier gas is increased, the highest dispersion field accessible decreases. This work presents the trade-offs between increasing dispersion fields and using helium in the carrier gas by comparing the separation of a mixture of isobaric peptides. The maximum resolution for a separation of a mixture of three peptides with the same nominal molar mass was achieved by using a high dispersion field (~72 kV/cm) with pure nitrogen as the carrier gas within the DIMS assembly. The conditions used to achieve the maximum resolution also exhibit the lowest ion transmission through the assembly, suggesting that it is necessary to consider the trade-off between sensitivity and resolution when optimizing DIMS conditions for a given application.
“…Because of its potential for complex mixture characterization, significant work has focused on improving IMS resolution capabilities; several high-resolution instruments are capable of resolving powers [defined as
, where t is the drift time of the ion and Δ t is the full width at half maximum (FWHM) of the peak] in the range of ~100 to ~200 [12, 29–36]. Higher resolution IMS measurements are possible [37–40] but are still at an early stage of development.…”
Complexation of a series of related amino compounds by 18-crown-6 ether (18C6) is studied as a means of improving the resolution of mixtures by combinations of ion mobility spectrometry (IMS) and mass spectrometry (MS) techniques. Mixtures of the isomeric amines n-octylamine (NOA), dibutylamine (DBA), and diisopropylethylamine (DIPEA) were electrosprayed to produce gaseous [M + H]+ ions. These species have overlapping mobilities and are not resolved by IMS. Addition of 18C6 yields [M + 18C6 + H]+ ion complexes that are resolved by IMS. In subsequent experiments, [M + 18C6 + H]+ ion complexes are separated according to their mobilities and specific species are selected and exposed to collisional activation. This analysis yields dissociation voltages that are inversely correlated with the number of separate substitutions on the nitrogen atom of the amino compounds; dissociation voltages of ~40, ~90, and ~150 V are obtained for the tri-, di-, and mono-substituted amino compounds DIPEA, DBA, and NOA, respectively. For these complexes, an inverse correlation is also observed with respect to the gas-phase basicities (GB) of the amino compounds (964, 935, and 895 kJ mol−1, respectively). Studies of 18C6 complexes with a series of n-alkylamines (CnH2n+3N where n=3 to 18, respectively) show that dissociation voltages increase systematically (from ~140 to ~190 V) under the conditions employed. The sensitivity to collision energy provides an additional means of distinguishing between classes of compounds. The approach is extended as a means of separating nitrogen-containing compounds from petroleum.
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