Abstract
Herein we report multiple ion mobility (IM) peaks in electrospray ionization IM mass spectrometry (ESI-IM-MS) produced by glutamine residue in peptide. The mobility features of 147 peptides were investigated using ESI-IM-MS combined with liquid chromatography. Of these peptides, 66 presented multiple IM peaks, and analysis of their sequence using collision induced dissociation (CID) revealed that glutamine (Gln), as well as proline (Pro), plays a critical role in generating multiple IM peaks. Mutant-based investigations using Gln-containing peptides indicate that the side chain of Gln promotes intermolecular interactions, inducing multiple structures of the peptide ions in the gas phase. Consequently, the present study demonstrates that the distinct ion mobility signatures identified herein can potentially be used to characterize glutamine-containing peptide ions.
Original language | English |
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Pages (from-to) | 137-145 |
Number of pages | 9 |
Journal | Mass Spectrometry Letters |
Volume | 12 |
Issue number | 4 |
DOIs | |
Publication status | Published - 2021 Dec |
Bibliographical note
Funding Information:This research was supported by a National Research Council of Science & Technology (NST) grant from the Korean Government (MSIP) (No. CAP-15-10-KRICT) and a Korea University Future Research Grant.
Publisher Copyright:
©Korean Society for Mass Spectrometry.
Keywords
- Glutamine
- Ion chemistry
- Ion mobility mass spectrometry
- Tryptic peptide
ASJC Scopus subject areas
- Analytical Chemistry
- General Biochemistry,Genetics and Molecular Biology
- Spectroscopy