Ion Mobility-Mass Spectrometry with a Radial Opposed Migration Ion and Aerosol Classifier (ROMIAC)
Abstract
The first application of a novel differential mobility analyzer, the radial opposed migration ion and aerosol classifier (ROMIAC), is demonstrated. The ROMIAC uses antiparallel forces from an electric field and a cross-flow gas to both scan ion mobilities and continuously transmit target mobility ions with 100% duty cycle. In the ROMIAC, diffusive losses are minimized, and resolution of ions, with collisional cross-sections of 200–2000 Å^2, is achieved near the nondispersive resolution of ~20. Higher resolution is theoretically possible with greater cross-flow rates. The ROMIAC was coupled to a linear trap quadrupole mass spectrometer and used to classify electrosprayed C2–C12 tetra-alkyl ammonium ions, bradykinin, angiotensin I, angiotensin II, bovine ubiquitin, and two pairs of model peptide isomers. Instrument and mobility calibrations of the ROMIAC show that it exhibits linear responses to changes in electrode potential, making the ROMIAC suitable for mobility and cross-section measurements. The high resolution of the ROMIAC facilitates separation of isobaric isomeric peptides. Monitoring distinct dissociation pathways associated with peptide isomers fully resolves overlapping peaks in the ion mobility data. The ability of the ROMIAC to operate at atmospheric pressure and serve as a front-end analyzer to continuously transmit ions with a particular mobility facilitates extensive studies of target molecules using a variety of mass spectrometric methods.
Additional Information
© 2013 American Chemical Society. Received: February 28, 2013; Accepted: June 4, 2013; Published: June 4, 2013. Andrew Metcalf, Xerxes Lopez-Yglesias, and Kate Upton are acknowledged for technical assistance with the LabView program and MS support. Financial support comes from a NSF Graduate Research Fellowship (W.M.); the Beckman Institute at Caltech (J.L.B. and D.A.T.); the Jacobs Institute for Molecular Engineering for Medicine (R.C.F. and A.J.D.). This work was supported by the National Science Foundation under Grant No. CBET-1236909.Attached Files
Supplemental Material - ac400580u_si_001.pdf
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Additional details
- Eprint ID
- 41026
- DOI
- 10.1021/ac400580u
- Resolver ID
- CaltechAUTHORS:20130830-103839195
- NSF Graduate Research Fellowship
- Caltech Beckman Institute
- Jacobs Institute for Molecular Engineering for Medicine
- NSF
- CBET-1236909
- Created
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2013-08-30Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field