A study of b1+H2O and b1-ions in the product ion spectra of dipeptides containing N-terminal basic amino acid residues

  • Richard D. Hiserodt
  • Sharon M. Brown
  • Dennis F. H. Swijter
  • Nicole Hawkins
  • Cynthia J. Mussinan
Articles

DOI: 10.1016/j.jasms.2007.04.018

Cite this article as:
Hiserodt, R.D., Brown, S.M., Swijter, D.F.H. et al. J Am Soc Mass Spectrom (2007) 18: 1414. doi:10.1016/j.jasms.2007.04.018

Abstract

The product ion spectra of approximately 200 dipeptides were acquired under low-energy conditions using a triple quadrupole mass spectrometer. The spectra of dipeptides containing an N-terminal arginine (R), histidine (H), or lysine (K) were observed to yield a b1 + H2O ion corresponding to the protonated basic amino acid. This was equivalent to the y1-ion in the corresponding C-terminal isomer. The formation of a b1 + H2O ion was not a significant fragmentation channel in any dipeptides analyzed including those containing a C-terminal basic amino acid unless they also contained an N-terminal basic amino acid. Occurring simultaneously and under equal energy conditions an apparent b1-ion was formed, which has its corresponding C-terminal equivalent in the y1-H2O ion. Energy resolved mass spectrometry (ERMS), deuterium labeling, and accurate mass experiments as well as data reported were used to show the relationships between the b1 + H2O and b1-ions in the dipeptides containing an N-terminal basic amino acid and the y1 and y1-H2O ions in the corresponding C-terminal isomers.

Copyright information

© American Society for Mass Spectrometry 2007

Authors and Affiliations

  • Richard D. Hiserodt
    • 1
  • Sharon M. Brown
    • 1
  • Dennis F. H. Swijter
    • 1
  • Nicole Hawkins
    • 1
  • Cynthia J. Mussinan
    • 1
  1. 1.Research and DevelopmentInternational Flavors and Fragrances Inc. (IFF)Union BeachUSA

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