Peptide peak intensities enhanced by cysteine modifiers and MALDI TOF MS

Masoud Zabet-Moghaddam, Aarif L. Shaikh, Satomi Niwayama

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

Two cysteine-specific modifiers we reported previously, N-ethyl maleimide (NEM) and iodoacetanilide (IAA), have been applied to the labeling of cysteine residues of peptides for the purpose of examining the enhancement of ionization efficiencies in combination with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI TOF MS). The peak intensities of the peptides as a result of modification with these modifiers were compared with the peak intensities of peptides modified with a commercially available cysteine-specific modifier, iodoacetamide (IA). Our experiments show significant enhancement in the peak intensities of three cysteine-containing synthetic peptides modified with IAA compared to those modified with IA. The results showed a 4.5-6-fold increase as a result of modification with IAA compared to modification with IA. Furthermore, it was found that IAA modification also significantly enhanced the peak intensities of many peptides of a commercially available proteins, bovine serum albumin (BSA), compared to those modified with IA. This significant enhancement helped identify a greater number of peptides of these proteins, leading to a higher sequence coverage with greater confidence scores in identification of proteins with the use of IAA.

Original languageEnglish
Pages (from-to)1546-1553
Number of pages8
JournalJournal of Mass Spectrometry
Volume47
Issue number12
DOIs
StatePublished - Dec 2012

Keywords

  • MALDI TOF
  • alkylation
  • cysteine modifier
  • ionization efficiencies
  • peak enhancement

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