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

  • Xiaojuan Li
  • Cheng Lin
  • Liang Han
  • Catherine E. Costello
  • Peter B. O’Connor
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.

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Copyright information

© American Society for Mass Spectrometry 2010

Authors and Affiliations

  • Xiaojuan Li
    • 1
  • Cheng Lin
    • 1
  • Liang Han
    • 1
    • 2
  • Catherine E. Costello
    • 1
  • Peter B. O’Connor
    • 1
    • 3
  1. 1.Mass Spectrometry Resource, Department of BiochemistryBoston University School of MedicineBostonUSA
  2. 2.Department of ChemistryBoston UniversityBostonUSA
  3. 3.Department of ChemistryUniversity of WarwickCoventryUK