Journal
ANALYTICAL CHEMISTRY
Volume 84, Issue 17, Pages 7297-7300Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ac3018636
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Funding
- Battelle Independent RD Program
- NIH NCRR [RR 018522]
- NIH NIGMS [8P41GM103493]
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Differential ion mobility spectrometry (FAIMS) integrated with mass spectrometry (MS) is a powerful new tool for biological and environmental analyses. Large proteins occupy regions of FAIMS spectra distinct from peptides, lipids, or other medium-size biomolecules, likely because strong electric fields align huge dipoles common to macroions. Here we confirm this phenomenon in separations of proteins at extreme fields using FAIMS chips coupled to MS and demonstrate their use to detect even minor amounts of large proteins in complex matrixes of smaller proteins and peptides.
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