Abstract

European Journal of Mass Spectrometry
Volume 12 Issue 4, Pages 213–221 (2006)
doi: 10.1255/ejms.814

A matrix-assisted laser desorption/ionization compatible reagent for tagging tryptophan residues

Chunyan Li, Vijay Gawandi, Adam Protos, Robert S. Phillips and I. Jonathan Amster^*
Department of Chemistry, University of Georgia, Athens, Georgia 30602, USA. E-mail: jamster@uga.edu

Chemical tagging of amino acids is an important tool in proteomics analysis, and has been used to introduce isotope labels and mass defect labels into proteolytic peptides by derivatization of cysteine or lysine residues. Here we present a new reagent with chemical specificity for tryptophan residues. Previously, 2-nitrobenzenesulfenyl chloride has been used as a highly specific reagent for labeling tryptophan residues. We show that this tag undergoes UV dissociation during MALDI. The multiplicity of photofragments increases the difficulty of characterizing the derivatization products. To overcome this problem, we have synthesized a new reagent, 2-(trifluoromethyl)benzenesulfenyl chloride, which is shown to react quantitatively with tryptophan in peptides and proteins. Most significantly, it exhibits high photostability in MALDI-FTMS analyses.

Keywords: tryptophan, photosensitivity, MALDI, 2- nitrobenzenesulfnenyl chloride, 2-(trifluoromethyl)benzenesulfenyl chloride

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