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Research Article
Identification of intermolecular disulfide linkages in underivatised peptides using negative ion electrospray mass spectrometry. A joint experimental and theoretical study
Article first published online: 5 FEB 2007
DOI: 10.1002/rcm.2872
Copyright © 2007 John Wiley & Sons, Ltd.
1097-0231/asset/cover.gif?v=1&s=685086e2b20ab07e9ab5ac022b9782ebdcd7ce5c "Rapid Communications in Mass Spectrometry")
Additional Information
How to Cite
Bilusich, D. and Bowie, J. H. (2007), Identification of intermolecular disulfide linkages in underivatised peptides using negative ion electrospray mass spectrometry. A joint experimental and theoretical study. Rapid Commun. Mass Spectrom., 21: 619–628. doi: 10.1002/rcm.2872
Publication History
- Issue published online: 5 FEB 2007
- Article first published online: 5 FEB 2007
- Manuscript Accepted: 12 DEC 2006
- Manuscript Revised: 7 DEC 2006
- Manuscript Received: 23 OCT 2006
Funded by
- The Australian Research Council
- Abstract
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- Cited By
Abstract
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H]− ion of a symmetrical peptide containing one intermolecular disulfide linkage cleaves through the disulfide link to produce up to four fragment anions. Two of these characteristic fragments are formed by a cleavage initiated from the Cys enolate anion on the peptide backbone. The other fragment anions are formed by a cleavage directed from an anion site on the disulfide side chain. In the case of an unsymmetrical peptide containing one intermolecular disulfide, the [MH]− anion may cleave through the disulfide unit to give a maximum of eight cleavage anions. These fragmentations are low-energy processes as determined by theoretical calculations carried out at the HF/6-31G(d)//AM1 level of theory. Collision-induced mass spectra of the fragment anions may provide the sequence of the peptide. Copyright © 2007 John Wiley & Sons, Ltd.