Research Article

Application of electron transfer dissociation mass spectrometry in analyses of non-enzymatically glycated peptides†‡

  1. Qibin Zhang1,
  2. Andrej Frolov2,
  3. Ning Tang3,
  4. Ralf Hoffmann2,
  5. Tom van de Goor3,
  6. Thomas O. Metz1,
  7. Richard D. Smith1,*

Article first published online: 5 FEB 2007

DOI: 10.1002/rcm.2884

Issue

Rapid Communications in Mass Spectrometry

Rapid Communications in Mass Spectrometry

Volume 21, Issue 5, pages 661–666, 15 March 2007

Additional Information

How to Cite

Zhang, Q., Frolov, A., Tang, N., Hoffmann, R., van de Goor, T., Metz, T. O. and Smith, R. D. (2007), Application of electron transfer dissociation mass spectrometry in analyses of non-enzymatically glycated peptides. Rapid Communications in Mass Spectrometry, 21: 661–666. doi: 10.1002/rcm.2884

Author Information

  1. 1

    Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA

  2. 2

    Bioanalytics, Center for Biotechnology and Biomedicine, Faculty of Chemistry and Mineralogy, University of Leipzig, Deutscher Platz, 04103 Leipzig, Germany

  3. 3

    Life Science & Chemical Analysis, Agilent Technologies, Santa Clara, CA 95052, USA

*Biological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA 99352, USA.

  1. †

    This article is a U.S. Government work and is in the public domain in the U.S.A.

  2. ‡

    Qibin Zhang and Andrej Frolov contributed equally to this work.

Publication History

  1. Issue published online: 5 FEB 2007
  2. Article first published online: 5 FEB 2007
  3. Manuscript Accepted: 21 DEC 2006
  4. Manuscript Revised: 7 DEC 2006
  5. Manuscript Received: 11 OCT 2006

Funded by

  • NIH. Grant Number: 5R21DK071283
  • National Center for Research Resources. Grant Number: RR018522
  • Deutsche Forschungsgemeinschaft. Grant Number: Graduiertenkolleg 378

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Abstract

Non-enzymatic glycation of peptides and proteins by D-glucose has important implications in the pathogenesis of diabetes mellitus, particularly in the context of development of diabetic complications. The fragmentation behavior of glycated peptides produced from reaction of D-glucose with lysine residues was investigated by electron transfer dissociation (ETD) and collision-induced dissociation (CID) tandem mass spectrometry. It was found that high abundance ions corresponding to various degrees of neutral water losses, as well as furylium ion production, dominate the CID spectra, and that the sequence-informative b and y ions were rarely observed when Amadori-modified peptides were fragmented. Contrary to what was observed under CID conditions, ions corresponding to neutral losses of water or furylium ion production were not observed in the ETD spectra. Instead, abundant and almost complete series of c- and z-type ions were observed regardless of whether the modification site was located in the middle of the sequence or close to the N-terminus, greatly facilitating the peptide sequencing. This study strongly suggests that ETD is a better technique for proteomic studies of non-enzymatically glycated peptides and proteins. Published in 2007 by John Wiley & Sons, Ltd.

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