ArticleAnalytical chemistry2011
Shift reagents for multidimensional ion mobility spectrometry-mass spectrometry analysis of complex peptide mixtures: evaluation of 18-crown-6 ether complexes.
Article in Analytical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Gas Phase Separation of Modified Peptides for Activity-Based Protein Profiling.Analytical chemistry · 2025Article
- Assessing the Use of Host-Guest Chemistry in Conjunction with Cyclic Ion Mobility Separations for the Linkage-Specific Characterization of Human Milk Oligosaccharides.International journal of mass spectrometry · 2023Article
- Recent advances in ion mobility-mass spectrometry for improved structural characterization of glycans and glycoconjugates.Current opinion in chemical biology · 2018Review
- Experimental evaluation and optimization of structures for lossless ion manipulations for ion mobility spectrometry with time-of-flight mass spectrometry.Analytical chemistry · 2014Article
- The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics.Nature chemistry · 2014Review
- Factors that influence competitive intermolecular solvation of protonated groups in peptides and proteins in the gas phase.Journal of the American Society for Mass Spectrometry · 2013Article
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Authors and funding
2 authors.
Funding
Abstract
18-Crown-6 ether (18C6) is evaluated as a shift reagent for multidimensional ion mobility spectrometry-mass spectrometry (IMS-IMS-MS) analyses of tryptic protein digests. In this approach, 18C6 is spiked into the solution-phase mixture and noncovalent peptide-crown ion complexes are formed by electrospraying the mixture into the gas phase. After an initial mobility separation in the first IMS drift region, complexes of similar mobility are selected and dissociated via collisional activation prior to entering the second drift region. These dissociation products (including smaller complexes, naked peptide ions, charge transfer products, and fragment ions) differ in mobility from their precursor ion complexes and (in favorable cases) from one another, allowing the mixture to resolve further in the second IMS region. We estimate an IMS-IMS peak capacity of ~2400 when shift reagents are employed. The approach is illustrated by examining a tryptic digest of cytochrome c and by identifying a peptide out of a complex mixture obtained by digestion of human plasma proteins. Disadvantages arising from increased complexity of data sets as well as other advantages of this approach are considered.
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