Tandem mass spectrometry of amidated peptides
Version of Record online: 30 OCT 2006
Copyright © 2006 John Wiley & Sons, Ltd.
Journal of Mass Spectrometry
Volume 41, Issue 11, pages 1470–1483, November 2006
How to Cite
Mouls, L., Subra, G., Aubagnac, J.-L., Martinez, J. and Enjalbal, C. (2006), Tandem mass spectrometry of amidated peptides. J. Mass Spectrom., 41: 1470–1483. doi: 10.1002/jms.1118
- Issue online: 10 NOV 2006
- Version of Record online: 30 OCT 2006
- Manuscript Accepted: 31 AUG 2006
- Manuscript Received: 28 APR 2006
- ammonia loss
The behavior of C-terminal amidated and carboxylated peptides upon low-energy collision-induced dissociation (CID) was investigated. Two sets of 76 sequences of variable amino acid compositions and lengths were synthesized as model compounds. In most cases, C-terminal amidated peptides were found to produce, upon CID, an abundant loss of ammonia from the protonated molecules. To validate such MS/MS signatures, the studied peptides contained amino acids that can potentially release ammonia from their side chains, such as asparagine, glutamine, tryptophan, lysine and arginine. Arginine, and to a lesser extent lysine, was shown to induce a competitive fragmentation leading to the loss of ammonia from their side chains, thus interfering with the targeted backbone neutral release. However, when arginine or lysine was located at the C-terminal position mimicking a tryptic digest, losses of ammonia from the arginine side chain and from the peptide backbone were completely suppressed. Such results were discussed in the frame of peptidomic or proteomic studies in an attempt to reveal the presence of C-terminal amidated peptides or proteins. Copyright © 2006 John Wiley & Sons, Ltd.