Ion Mobility-Mass Spectrometry with a Radial Opposed Migration Ion and Aerosol Classifier (ROMIAC)

被引:11
作者
Mui, Wilton [1 ]
Thomas, Daniel A. [2 ]
Downard, Andrew J. [2 ]
Beauchamp, Jesse L. [2 ]
Seinfeld, John H. [1 ,2 ]
Flagan, Richard C. [1 ,2 ]
机构
[1] CALTECH, Div Engn & Appl Sci, Pasadena, CA 91125 USA
[2] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA
基金
美国国家科学基金会;
关键词
GAS-PHASE; ELECTROSPRAY-IONIZATION; HIGH-RESOLUTION; PROTEIN COMPLEXES; ELECTROPHORETIC MOBILITY; PARTICLE CLASSIFICATION; CROSS-SECTION; BRADYKININ; CONFORMERS; ANALYZERS;
D O I
10.1021/ac400580u
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
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 angstrom(2), is achieved near the nondispersive resolution of similar to 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.
引用
收藏
页码:6319 / 6326
页数:8
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