Details

Autor(en) / Beteiligte

• Hao, Gang
• Wang, Danchen
• Gu, Jane
• Shen, Qiuying
• Gross, Steven S.
• Wang, Yanming

Titel

Neutral Loss of Isocyanic Acid in Peptide CID Spectra: A Novel Diagnostic Marker for Mass Spectrometric Identification of Protein Citrullination

Ist Teil von

• Journal of the American Society for Mass Spectrometry, 2009-04, Vol.20 (4), p.723-727

Ort / Verlag

New York: Elsevier Inc

Erscheinungsjahr

2009

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Protein citrullination is emerging as an important signaling mechanism that modulates a variety of biological processes. This protein modification constitutes only a 1 Da mass shift, and can be readily confused with other common protein modifications that yield an identical mass shift. In an attempt to develop a robust methodology for detection of protein citrullination sites, we analyzed synthetic citrulline-containing peptides by electrospray ionization tandem mass spectrometry. Collision-induced dissociation (CID) spectra revealed abundant neutral loss of 43 Da from citrullinated peptide precursor ions, which was reconciled by elimination of the HNCO moiety (isocyanic acid) from the citrulline ureido group. The elimination occurs readily in multiple charge states of precursor ions and also in b and y ions. HNCO loss in CID spectra provides a novel diagnostic marker for citrullination, and its utility was demonstrated by the discovery of Arg197 as the specific site of citrullination on nucleophosmin upon peptidylarginine deiminase 4 treatment. Gas-phase elimination of isocyanic acid from citrulline containing peptides.