Development of a Fourier-transform ion cyclotron resonance mass spectrometer-ion mobility spectrometer

Bluhm, Brian K.; Gillig, Kent J.; Russell, David H.

doi:10.1063/1.1288235

Cited by 55 publications

(30 citation statements)

References 34 publications

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“…According to the theoretical constructs presented here, a decrease in ion mobility will only aid the acquisition of low-field, diffusion-limited resolution. Monte Carlo simulations performed in our laboratory indicate that the transmission efficiency decrease due to increased radial diffusion under highfield separation conditions is minimal for peptides and proteins, and that ion losses due to diffusion can be further mitigated by the application of ion guide-type IM drift tube designs [22,27,28]. In general, the results presented here clearly illustrate that operating IM separations at high E/p facilitate faster separation times, i.e., higher throughput, without loss in resolution for applications in proteomics.…”

Section: Discussionmentioning

confidence: 99%

Resolution equations for high-field ion mobility

Verbeck

Ruotolo

Gillig

et al. 2004

J. Am. Soc. Mass Spectrom.

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An extension of current mobility resolution equations as they apply to high-field ion mobility spectrometry is presented. The new resolution expression is applied to arrival time distributions for ions having a large range of ion mobilities and mass-to-charge ratios (m/z). The results indicate that the new equation can be utilized to predict the mobility resolution over a broader range of applied electric fields than previous ion mobility resolution expressions. (J Am Soc Mass Spectrom 2004, 15, 1320 -1324) © 2004 American Society for Mass Spectrometry S eparation based on the mobility of an ion through a neutral buffer gas (i.e., ion mobility spectrometry (IMS)) [1,2] is an important technology for studying long-lived electronic states of gas-phase ions and a sensitive method for detection of air-borne species [3, 4]. Recent work, which demonstrates the utility of IMS for analyzing gas-phase ionized biopolymers (i.e., peptides, proteins, DNA, etc.), has renewed interest in the analytical applications of IMS and led to the development of several high-resolution drift tubes in combination with mass spectrometry [5][6][7][8][9][10][11]. In order to perform a gas-phase separation of near thermal, structurally isomeric gas-phase ion populations, most IMS separations are performed near the low-field limit. Low-field conditions are important for studies of gas-phase peptide/protein structure because collisional activation can, in some cases, lead to structural rearrangement and/or fragmentation.In addition to the distinctions drawn for IMS operation in terms of separation field strength, the use of IMS can be divided into two pressure regimes, viz. high pressure (typically low-field) and low pressure (either low or high applied fields), and there are distinct advantages associated with both pressure regimes. At high pressure, the number of ion-neutral collisions is high, i.e., C 60 ϩ⅐ undergoes 10 10 collisions/s at 760 torr He compared with about 10 7 collisions/s for the same ion at 1 torr He. It is also important to consider that collisions with low-level impurities may significantly influence the separation and total drift time of an analyte ion. For example, in a 30 cm drift cell maintained at 760 torr He, C 60 ϩ⅐ will undergo 10 5 -10 6 collisions with a of 0.01% impurity, compared with ca. 10 collisions with the same level of impurity at 1 torr He. Another advantage of low-pressure drift tubes is the ease of coupling ion mobility with high vacuum mass spectrometers. Lastly, low-pressure (or high-field) mobility decreases ion separation times, leading to higher throughput analysis (approximately 3 orders of magnitude faster for analysis times at 1 torr over 760 torr).Low-field mobility conditions are defined in terms of the kinetic energy acquired by the ion in the presence of an applied field (E o ). That is, the translational energy gained by the ion between collisions should be less than the thermal energy of the collision gas [12, 13],where m is the mass of the ion, M is the mass of the neutral drift gas, ...

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Section: Discussionmentioning

confidence: 99%

Resolution equations for high-field ion mobility

Verbeck

Ruotolo

Gillig

et al. 2004

J. Am. Soc. Mass Spectrom.

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“…If the temporal separation between "eluting" components exceeds the MS analysis timescale, a mass spectrometer joined to the IMS terminus can probe the components one at a time. IMS has now been coupled to quadrupole MS [10], time-of-flight MS [13], and FTICR [14]. The IMS/TOF hybrid that disperses analyte mixtures in mobility and mass dimensions simultaneously is a promising new platform for high-throughput analytical applications [15,16].…”

mentioning

confidence: 99%

Modeling the resolution and sensitivity of FAIMS analyses

Shvartsburg

Tang

Smith

2004

J. Am. Soc. Mass Spectrom.

102

216

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Field asymmetric waveform ion mobility spectrometry (FAIMS) is rapidly gaining acceptance as a robust, versatile tool for post-ionization separations prior to mass-spectrometric analyses. The separation is based on differences between ion mobilities at high and low electric fields, and proceeds at atmospheric pressure. Two major advantages of FAIMS over condensedphase separations are its high speed and an ion focusing effect that often improves sensitivity. While selected aspects of FAIMS performance are understood empirically, no physical model rationalizing the resolving power and sensitivity of the method and revealing their dependence on instrumental variables has existed. Here we present a first-principles computational treatment capable of simulating the FAIMS analyzer for virtually any geometry (including the known cylindrical and planar designs) and arbitrary operational parameters. The approach involves propagating an ensemble of ion trajectories through the device in real time under the influence of applied asymmetric potential, diffusional motion incorporating the high-field and anisotropic phenomena, and mutual Coulomb repulsion of ionic charges. Calculations for both resolution and sensitivity are validated by excellent agreement with measurements in different FAIMS modes for ions representing diverse types and analyte classes. (J Am Soc Mass

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“…Data were collected and processed in an ioncounting mode by means of an Ionwerks time-to-digital converter (Model TDCX4). They also designed a Fouriertransform ion cyclotron resonance mass spectrometer-ion mobility spectrometer with TOFMS detection [54]. Also recently, Lee et al [55] developed an IMS-TOFMS instrument with an Ionwerks data system (Model TDCX4) and a Jaguar TOFMS (LECO, St. Joseph, MI, USA).…”

Section: Ims-ms Developments and Applicationsmentioning

confidence: 99%

Developments in ion mobility spectrometry–mass spectrometry

2001

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Ion mobility spectrometry (IMS) has been used for over 30 years as a sensitive detector of organic compounds. The following is a brief review of IMS and its principles with an emphasis on its usage when coupled to mass spectrometry. Since its inception, IMS has been interfaced with quadrupole, time-of-flight, and Fourier-transform ion cyclotron resonance mass spectrometry. These hybrid instruments have been employed for the analysis of a variety of target analytes, including biomolecules, explosives, chemical warfare degradation products, and illicit drugs.

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Development of a Fourier-transform ion cyclotron resonance mass spectrometer-ion mobility spectrometer

Cited by 55 publications

References 34 publications

Resolution equations for high-field ion mobility

Resolution equations for high-field ion mobility

Modeling the resolution and sensitivity of FAIMS analyses

Developments in ion mobility spectrometry–mass spectrometry

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