Journal of the American Society for Mass Spectrometry

, Volume 21, Issue 4, pp 646–656

Charge remote fragmentation in electron capture and electron transfer dissociation

Authors

  • Xiaojuan Li
    • Mass Spectrometry Resource, Department of BiochemistryBoston University School of Medicine
  • Cheng Lin
    • Mass Spectrometry Resource, Department of BiochemistryBoston University School of Medicine
  • Liang Han
    • Mass Spectrometry Resource, Department of BiochemistryBoston University School of Medicine
    • Department of ChemistryBoston University
  • Catherine E. Costello
    • Mass Spectrometry Resource, Department of BiochemistryBoston University School of Medicine
    • Mass Spectrometry Resource, Department of BiochemistryBoston University School of Medicine
    • Department of ChemistryUniversity of Warwick
Article

DOI: 10.1016/j.jasms.2010.01.001

Cite this article as:
Li, X., Lin, C., Han, L. et al. J Am Soc Mass Spectrom (2010) 21: 646. doi:10.1016/j.jasms.2010.01.001

Abstract

Secondary fragmentations of three synthetic peptides (human αA crystallin peptide 1-11, the deamidated form of human βB2 crystallin peptide 4-14, and amyloid β peptide 25-35) were studied in both electron capture dissociation (ECD) and electron-transfer dissociation (ETD) mode. In ECD, in addition to c and z· ion formations, charge remote fragmentations (CRF) of z· ions were abundant, resulting in internal fragment formation or partial/entire side-chain losses from amino acids, sometimes several residues away from the backbone cleavage site, and to some extent multiple side-chain losses. The internal fragments were observed in peptides with basic residues located in the middle of the sequences, which was different from most tryptic peptides with basic residues located at the C-terminus. These secondary cleavages were initiated by hydrogen abstraction at the α-, β-, or γ-position of the amino acid side chain. In comparison, ETD generates fewer CRF fragments than ECD. This secondary cleavage study will facilitate ECD/ETD spectra interpretation, and help de novo sequencing and database searching.

Supplementary material

13361_2011_210400646_MOESM1_ESM.ppt (43 kb)
Supplementary material, approximately 44 KB.
13361_2011_210400646_MOESM2_ESM.doc (516 kb)
Supplementary material, approximately 528 KB.
13361_2011_210400646_MOESM3_ESM.ppt (42 kb)
Supplementary material, approximately 43 KB.

Copyright information

© American Society for Mass Spectrometry 2010