Quantitative analysis of relative amounts of expressed proteins and identification of the proteins in combination with mass spectrometry are central to proteomics studies.  We have thus far reported five kinds of reagents that react with specific amino acid residues and their d- or 13C-labeled versions which can successfully measure the relative amounts of peptides or proteins in combination with electrophoresis and soft ionization mass spectrometry such as MALDI or ESI.  However, most of the reagents we reported in the past rely on the existence of cysteine residues.  Here we report synthesis of a new modifier, 2-ethyl succinic anhydride (ESA), which reacts with the amino group and its d5-labeled version, and the application of their combination to quantitative analysis of peptides in combination with MALDI TOF mass spectrometry.This study finds that this combination enables quantitative analysis of model peptides with high accuracy.  As this method does not require the existence of particular amino acid residues, it is expected to be applicable to quantitative analysis of a wider variety of proteins.  These modifiers can also be prepared relatively inexpensively from readily available sources.  This study provides an additional method for quantitative analysis of peptides and proteins, which is important for proteomics studies.

Synthesis of d-labeled and unlabeled ethyl succinic anhydride and application to quantitative analysis of peptides by isotope differential mass spectrometry

246th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.