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Article: Fragmentation of α-Radical Cations of Arginine-Containing Peptides

TitleFragmentation of α-Radical Cations of Arginine-Containing Peptides
Authors
Issue Date2010
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jasms
Citation
Journal Of The American Society For Mass Spectrometry, 2010, v. 21 n. 4, p. 511-521 How to Cite?
AbstractFragmentation pathways of peptide radical cations, M +·, with well-defined initial location of the radical site were explored using collision-induced dissociation (CID) experiments. Peptide radical cations were produced by gas-phase fragmentation of Co III(salen)-peptide complexes [salen = N,N'-ethylenebis (salicylideneiminato)]. Subsequent hydrogen abstraction from the β-carbon of the side-chain followed by C α-C β bond cleavage results in the loss of a neutral side chain and formation of an α-radical cation with the radical site localized on the α-carbon of the backbone. Similar CID spectra dominated by radical-driven dissociation products were obtained for a number of arginine-containing α-radicals, suggesting that for these systems radical migration precedes fragmentation. In contrast, proton-driven fragmentation dominates CID spectra of α-radicals produced via the loss of the arginine side chain. Radical-driven fragmentation of large M + peptide radical cations is dominated by side-chain losses, formation of even-electron a-ions and odd-electron x-ions resulting from C α-C bond cleavages, formation of odd-electron z-ions, and loss of the N-terminal residue. In contrast, charge-driven fragmentation produces even-electron y-ions and odd-electron b-ions. © 2010 American Society for Mass Spectrometry.
Persistent Identifierhttp://hdl.handle.net/10722/135030
ISSN
2015 Impact Factor: 3.031
2015 SCImago Journal Rankings: 1.322
ISI Accession Number ID
Funding AgencyGrant Number
US DOE
University of Hong Kong
Funding Information:

The authors acknowledge partial support for this study by a grant from the Chemical Sciences Division, Office of Basic Energy Sciences of the US DOE and partially by the University of Hong Kong and Hong Kong Research Grant Council, Special Administrative Region, China (project nos. 7018/06P and 7012/08P). The research described in this manuscript was performed at the W. R. Wiley Environmental Molecular Sciences Laboratory (EMSL), a national scientific user facility sponsored by the U.S. Department of Energy's Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory (PNNL). PNNL is operated by Battelle for the U.S. Department of Energy. I.K.C. acknowledges participation in the PNNL Interfacial and Condensed Phase Summer Research Institute.

References

 

DC FieldValueLanguage
dc.contributor.authorLaskin, Jen_HK
dc.contributor.authorYang, Zen_HK
dc.contributor.authorNg, CMDen_HK
dc.contributor.authorChu, IKen_HK
dc.date.accessioned2011-07-27T01:26:16Z-
dc.date.available2011-07-27T01:26:16Z-
dc.date.issued2010en_HK
dc.identifier.citationJournal Of The American Society For Mass Spectrometry, 2010, v. 21 n. 4, p. 511-521en_HK
dc.identifier.issn1044-0305en_HK
dc.identifier.urihttp://hdl.handle.net/10722/135030-
dc.description.abstractFragmentation pathways of peptide radical cations, M +·, with well-defined initial location of the radical site were explored using collision-induced dissociation (CID) experiments. Peptide radical cations were produced by gas-phase fragmentation of Co III(salen)-peptide complexes [salen = N,N'-ethylenebis (salicylideneiminato)]. Subsequent hydrogen abstraction from the β-carbon of the side-chain followed by C α-C β bond cleavage results in the loss of a neutral side chain and formation of an α-radical cation with the radical site localized on the α-carbon of the backbone. Similar CID spectra dominated by radical-driven dissociation products were obtained for a number of arginine-containing α-radicals, suggesting that for these systems radical migration precedes fragmentation. In contrast, proton-driven fragmentation dominates CID spectra of α-radicals produced via the loss of the arginine side chain. Radical-driven fragmentation of large M + peptide radical cations is dominated by side-chain losses, formation of even-electron a-ions and odd-electron x-ions resulting from C α-C bond cleavages, formation of odd-electron z-ions, and loss of the N-terminal residue. In contrast, charge-driven fragmentation produces even-electron y-ions and odd-electron b-ions. © 2010 American Society for Mass Spectrometry.en_HK
dc.languageengen_US
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jasmsen_HK
dc.relation.ispartofJournal of the American Society for Mass Spectrometryen_HK
dc.subject.meshArginine - chemistry-
dc.subject.meshGas Chromatography-Mass Spectrometry - methods-
dc.subject.meshModels, Chemical-
dc.subject.meshPeptides - chemistry-
dc.subject.meshSpectrometry, Mass, Electrospray Ionization - methods-
dc.titleFragmentation of α-Radical Cations of Arginine-Containing Peptidesen_HK
dc.typeArticleen_HK
dc.identifier.emailChu, IK:ivankchu@hku.hken_HK
dc.identifier.authorityChu, IK=rp00683en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jasms.2009.12.021en_HK
dc.identifier.pmid20138543-
dc.identifier.scopuseid_2-s2.0-77950337558en_HK
dc.identifier.hkuros186324en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77950337558&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume21en_HK
dc.identifier.issue4en_HK
dc.identifier.spage511en_HK
dc.identifier.epage521en_HK
dc.identifier.isiWOS:000276788700003-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLaskin, J=7102409836en_HK
dc.identifier.scopusauthoridYang, Z=7405435606en_HK
dc.identifier.scopusauthoridNg, CMD=55107694700en_HK
dc.identifier.scopusauthoridChu, IK=7103327484en_HK
dc.identifier.citeulike6536196-

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