A study of peptide-peptide interactionsusing MALDI ion mobility o-TOF and ESImass spectrometry

Amina S. Woods, John M. Koomen, Brandon T. Ruotolo, Kent J. Gillig, David H. Russel, Katrin Fuhrer, Marc Gonin, Thomas F. Egan, J. Albert Schultz

Research output: Contribution to journalArticlepeer-review

Abstract

Matrix-assisted laser desorption ionization ion mobility coupled to orthogonal time-of-flight mass spectrometry (MALDI-IM-oTOF MS) is evaluated as a tool for studying non-covalent complex (NCX) formation between peptides. The NCX formed between dynorphin 1-7 and Mini Gastrin I is used as a model system for comparison to previous MALDI experiments (Woods, A. S.; Huestis, M. A. J. Am. Soc. Mass Spectrom. 2001, 12, 88-96). The dynorphin 1-7/Mini Gastrin I complex is stable after more than a ms drift time through the He filled mobility cell. Furthermore, the effects of solution pH on NCX ion signal intensity is measured both by MALDI-IM-MS analysis and by nanoelectrospray mass spectrometry. When compared to the previous MALDI study this work shows that all three techniques give similar results. In addition, fragmentation can be observed from of the non-covalent complex parent ion that occurs prior to TOF mass analysis but after mobility separation, thus providing NCX composition information.

Original languageEnglish (US)
Pages (from-to)166-169
Number of pages4
JournalJournal of the American Society for Mass Spectrometry
Volume13
Issue number2
DOIs
StatePublished - 2002
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Spectroscopy

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