Characterization of an N-acylated glucagon-like peptide-1 derivative by electron capture dissociation

  • Kim F. Haselmann
  • Per F. Nielsen
  • Roman A. Zubarev
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DOI: 10.1016/j.jasms.2005.01.009

Cite this article as:
Haselmann, K.F., Nielsen, P.F. & Zubarev, R.A. J Am Soc Mass Spectrom (2005) 16: 548. doi:10.1016/j.jasms.2005.01.009

Abstract

An N-acylated glucagon-like peptide 1 derivative was characterized by Fourier transform ion cyclotron resonance mass spectrometry. Both electron capture dissociation (ECD) and sustained off-resonance irradiation collisionally activated dissociation (SORI-CAD) were employed. While ECD revealed full sequence coverage, site of modification, branching point, structure of the palmitoylated modification, SORI-CAD produced less complete and more ambiguous information attributable to facile losses of the fatty acid group from both parent and fragments. Thus, ECD showed a superior characterization performance over SORI-CAD in analysis of N-acylated polypeptides.

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© American Society for Mass Spectrometry 2005

Authors and Affiliations

  • Kim F. Haselmann
    • 1
  • Per F. Nielsen
    • 2
  • Roman A. Zubarev
    • 3
  1. 1.Department of ChemistryUniversity of Southern DenmarkOdenseDenmark
  2. 2.Novo Nordisk A/SProtein ScienceBagsværdDenmark
  3. 3.Laboratory for Biological and Medical Mass Spectrometry, Uppsala Biomedical CenterUppsala UniversityUppsalaSweden