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Article: Formation of Anionic Peptide Radicals In Vacuo

TitleFormation of Anionic Peptide Radicals In Vacuo
Authors
Issue Date2006
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, 2006, v. 17 n. 9, p. 1249-1257 How to Cite?
AbstractIn this paper, we demonstrate for the first time the formation of radical anionic peptides [M - 2H] ·- through a one-electron transfer mechanism upon low-energy collision-induced dissociation (CID) of gas-phase singly charged [Mn III(salen)(M - 2H)] ·- complex ions [where salen is N,N′-ethylenebis(salicylideneiminato) and M is an angiotensin III derivative]. The types of fragment ions formed from [M - 2H] ·- share some similarities with those from the cationic radical peptides M ·+ and [M + H] ·2+, but differ significantly from those of the corresponding deprotonated peptides [M - H] -. Fragmentation of [M - 2H] ·- radical anionic angiotensin III derivatives leads preferentially to product ions of side-chain cleavage of amino acid residues, z-type and minor x-type fragment ions, most of which are types rarely observed in low-energy CID spectra of deprotonated analogs. The degree of competitive dissociation of the complexes is highly dependent on the nature of the substituted salen derivatives. The yields of anionic peptide radicals were enhanced to the greatest extent when electron withdrawing groups were positioned at the 5 and 5′ positions, but the effect was rather modest when such groups resided at the 3 and 3′ positions. Substituting a cyclohexyl unit of a salen with phenyl or naphthyl moieties at the 8 and 8′ positions also facilitated electron-transfer pathways. © 2006 American Society for Mass Spectrometry.
Persistent Identifierhttp://hdl.handle.net/10722/69585
ISSN
2015 Impact Factor: 3.031
2015 SCImago Journal Rankings: 1.322
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLam, CNWen_HK
dc.contributor.authorChu, IKen_HK
dc.date.accessioned2010-09-06T06:15:01Z-
dc.date.available2010-09-06T06:15:01Z-
dc.date.issued2006en_HK
dc.identifier.citationJournal Of The American Society For Mass Spectrometry, 2006, v. 17 n. 9, p. 1249-1257en_HK
dc.identifier.issn1044-0305en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69585-
dc.description.abstractIn this paper, we demonstrate for the first time the formation of radical anionic peptides [M - 2H] ·- through a one-electron transfer mechanism upon low-energy collision-induced dissociation (CID) of gas-phase singly charged [Mn III(salen)(M - 2H)] ·- complex ions [where salen is N,N′-ethylenebis(salicylideneiminato) and M is an angiotensin III derivative]. The types of fragment ions formed from [M - 2H] ·- share some similarities with those from the cationic radical peptides M ·+ and [M + H] ·2+, but differ significantly from those of the corresponding deprotonated peptides [M - H] -. Fragmentation of [M - 2H] ·- radical anionic angiotensin III derivatives leads preferentially to product ions of side-chain cleavage of amino acid residues, z-type and minor x-type fragment ions, most of which are types rarely observed in low-energy CID spectra of deprotonated analogs. The degree of competitive dissociation of the complexes is highly dependent on the nature of the substituted salen derivatives. The yields of anionic peptide radicals were enhanced to the greatest extent when electron withdrawing groups were positioned at the 5 and 5′ positions, but the effect was rather modest when such groups resided at the 3 and 3′ positions. Substituting a cyclohexyl unit of a salen with phenyl or naphthyl moieties at the 8 and 8′ positions also facilitated electron-transfer pathways. © 2006 American Society for Mass Spectrometry.en_HK
dc.languageengen_HK
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.rightsJournal of the American Society for Mass Spectrometry. Copyright © Elsevier Inc.en_HK
dc.titleFormation of Anionic Peptide Radicals In Vacuoen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1044-0305&volume=17&spage=1249&epage=1257&date=2006&atitle=Formation+of+anionic+peptide+radicals+in+vacuoen_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.2006.05.008en_HK
dc.identifier.pmid16809047-
dc.identifier.scopuseid_2-s2.0-33747887283en_HK
dc.identifier.hkuros119580en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33747887283&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume17en_HK
dc.identifier.issue9en_HK
dc.identifier.spage1249en_HK
dc.identifier.epage1257en_HK
dc.identifier.isiWOS:000240579200007-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLam, CNW=7402990888en_HK
dc.identifier.scopusauthoridChu, IK=7103327484en_HK

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