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Lookup NU author(s): Dr Achim Treumann
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Since its introduction, isobaric peptide labeling has played an important role in relative quantitative comparisons of proteomes. This paper describes isobaric peptide termini labeling (IPTL), a novel approach for the identification and quantification of two differentially labeled states using MS/MS spectra. After endoproteinase Lys-C digestion, peptides were labeled at C-terminal lysine residues with either 2-methoxy-4,5-dihydro-1H-imidazole (MDHI) or with tetradeuterated MDHI-d4. Subsequently, their N-termini were derivatized either with tetradeuterated succinic anhydride (SA-d4) or with SA. The mixed isotopic labeling results in isobaric masses and provided several quantification data points per peptide. The suitability of this approach is demonstrated with MS and MS/MS analyses of Lys-C digests of standard proteins. A conceptually simple quantification strategy with a dynamic range of 25 is achieved through the use of Mascot score ratios. The utility of IPTL for the analysis of proteomes was verified by comparing the well-characterized effect of the antimitotic inhibitor S-Trityl-L-Cysteine (STLC) on HeLa cells that were treated for either 24 or 48 h with the inhibitor. Many apoptosis-linked proteins were identified as being differentially regulated, confirming the suitability of IPTL for the analysis of complex proteomes. © 2009 American Chemical Society.
Author(s): Koehler C, Strozynski M, Kozielski F, Treumann A, Thiede B
Publication type: Article
Publication status: Published
Journal: Journal of Proteome Research
Year: 2009
Volume: 8
Issue: 9
Pages: 4333-4341
ISSN (print): 1535-3893
ISSN (electronic): 1535-3907
Publisher: American Chemical Society
URL: http://dx.doi.org/10.1021/pr900425n
DOI: 10.1021/pr900425n
PubMed id: 19655813
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