Studies of peptide a- and b-type fragment ions using stable isotope labeling and integrated ion mobility/tandem mass spectrometry

Isabel Riba Garcia, Kevin Giles, Robert H Bateman, Simon J Gaskell

Research output: Contribution to journalArticlepeer-review

Abstract

The structures of peptide a- and b-type fragment ions were studied using synthetic peptides including a set of isomeric peptides, differing in the sequence location of an alanine residue labeled with (15)N and uniformly with (13)C. The pattern of isotope labeling of second-generation fragment ions derived via a(n) and b(n) ions (where n = 4 or 5) suggested that these intermediates existed in part as macrocyclic structures, where alternative sites of ring opening gave rise to different linear forms whose simple cleavage might give rise to the observed final products. Similar conclusions were derived from combined ion mobility/tandem MS analyses where different fragmentation patterns were observed for isomeric a- or b-type ions that display different ion mobilities. These analyses were facilitated by a new approach to the processing of ion mobility/tandem MS data, from which distinct and separate product ion spectra are derived from ions that are incompletely separated by ion mobility. Finally, an example is provided of evidence for a macrocyclic structure for b(n) ions where n = 8 or 9.

Original languageEnglish
Pages (from-to)1781-7
Number of pages7
JournalJournal of the American Society for Mass Spectrometry
Volume19
Issue number12
DOIs
Publication statusPublished - Dec 2008

Keywords

  • Alanine
  • Amino Acid Sequence
  • Carbon Isotopes
  • Endorphins
  • Humans
  • Ions
  • Molecular Structure
  • Nitrogen Isotopes
  • Oligopeptides
  • Peptide Fragments
  • Tachykinins
  • Tandem Mass Spectrometry

Fingerprint

Dive into the research topics of 'Studies of peptide a- and b-type fragment ions using stable isotope labeling and integrated ion mobility/tandem mass spectrometry'. Together they form a unique fingerprint.

Cite this