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Article: Effect of the N-terminal basic residue on facile C α-C bond cleavages of aromatic-containing peptide radical cations

TitleEffect of the N-terminal basic residue on facile C α-C bond cleavages of aromatic-containing peptide radical cations
Authors
KeywordsCation
Peptide
Chemical structure
Mass spectrometry
Quantum theory
Issue Date2011
PublisherRoyal Society of Chemistry. The Journal's web site is located at http://www.rsc.org/pccp
Citation
Physical Chemistry Chemical Physics, 2011, v. 13 n. 13, p. 5888-5896 How to Cite?
AbstractFragmentation of radical cationic peptides [R(G) n-2X(G) 7-n] + and [R(G) m-2XG] + (X = Phe or Tyr; m = 2-5; n = 2-7) leads selectively to a n + product ions through in situ C α-C peptide backbone cleavage at the aromatic amino acid residues. In contrast, substituting the arginine residue with a less-basic lysine residue, forming [K(G) n-2X(G) 7-n] + (X = Phe or Tyr; n = 2-7) analogs, generates abundant b-y product ions; no site-selective C α-C peptide bond cleavage was observed. Studying the prototypical radical cationic tripeptides [RFG] + and [KFG] + using low-energy collision-induced dissociation and density functional theory, we have examined the influence of the basicity of the N-terminal amino acid residue on the competition between the isomerization and dissociation channels, particularly the selective C α-C bond cleavage via β-hydrogen atom migration. The dissociation barriers for the formation of a 2 + ions from [RFG] + and [KFG] +via their β-radical isomers are comparable (33.1 and 35.0 kcal mol -1, respectively); the dissociation barrier for the charge-induced formation of the [b 2 - H] + radical cation from [RFG] +via its α-radical isomer (39.8 kcal mol -1) was considerably higher than that from [KFG] + (27.2 kcal mol -1). Thus, the basic arginine residue sequesters the mobile proton to promote the charge-remote selective C α-C bond cleavage by energetically hindering the competing charge-induced pathways. © the Owner Societies. 2011.
Persistent Identifierhttp://hdl.handle.net/10722/135023
ISSN
2015 Impact Factor: 4.449
2015 SCImago Journal Rankings: 1.836
ISI Accession Number ID
Funding AgencyGrant Number
Hong Kong Research Grants CouncilHKU7012/08P
HKU7016/10P
Hong Kong Special Administrative Region, China
Hong Kong RGC
City University of Hong KongSRG7002552
Funding Information:

This study was supported by the Hong Kong Research Grants Council (Project No. HKU7012/08P and HKU7016/10P), Hong Kong Special Administrative Region, China. M.X., S.T., and Q.Q. thank the Hong Kong RGC for supporting their studentships. C.K. thanks City University of Hong Kong for financial support (SRG7002552).

References

 

DC FieldValueLanguage
dc.contributor.authorXu, Men_HK
dc.contributor.authorSong, Ten_HK
dc.contributor.authorQuan, Qen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorFang, DCen_HK
dc.contributor.authorSiu, CKen_HK
dc.contributor.authorChu, IKen_HK
dc.date.accessioned2011-07-27T01:26:13Z-
dc.date.available2011-07-27T01:26:13Z-
dc.date.issued2011en_HK
dc.identifier.citationPhysical Chemistry Chemical Physics, 2011, v. 13 n. 13, p. 5888-5896en_HK
dc.identifier.issn1463-9076en_HK
dc.identifier.urihttp://hdl.handle.net/10722/135023-
dc.description.abstractFragmentation of radical cationic peptides [R(G) n-2X(G) 7-n] + and [R(G) m-2XG] + (X = Phe or Tyr; m = 2-5; n = 2-7) leads selectively to a n + product ions through in situ C α-C peptide backbone cleavage at the aromatic amino acid residues. In contrast, substituting the arginine residue with a less-basic lysine residue, forming [K(G) n-2X(G) 7-n] + (X = Phe or Tyr; n = 2-7) analogs, generates abundant b-y product ions; no site-selective C α-C peptide bond cleavage was observed. Studying the prototypical radical cationic tripeptides [RFG] + and [KFG] + using low-energy collision-induced dissociation and density functional theory, we have examined the influence of the basicity of the N-terminal amino acid residue on the competition between the isomerization and dissociation channels, particularly the selective C α-C bond cleavage via β-hydrogen atom migration. The dissociation barriers for the formation of a 2 + ions from [RFG] + and [KFG] +via their β-radical isomers are comparable (33.1 and 35.0 kcal mol -1, respectively); the dissociation barrier for the charge-induced formation of the [b 2 - H] + radical cation from [RFG] +via its α-radical isomer (39.8 kcal mol -1) was considerably higher than that from [KFG] + (27.2 kcal mol -1). Thus, the basic arginine residue sequesters the mobile proton to promote the charge-remote selective C α-C bond cleavage by energetically hindering the competing charge-induced pathways. © the Owner Societies. 2011.en_HK
dc.languageengen_US
dc.publisherRoyal Society of Chemistry. The Journal's web site is located at http://www.rsc.org/pccpen_HK
dc.relation.ispartofPhysical Chemistry Chemical Physicsen_HK
dc.subjectCation-
dc.subjectPeptide-
dc.subjectChemical structure-
dc.subjectMass spectrometry-
dc.subjectQuantum theory-
dc.titleEffect of the N-terminal basic residue on facile C α-C bond cleavages of aromatic-containing peptide radical cationsen_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.doi10.1039/c0cp00974aen_HK
dc.identifier.pmid21327275-
dc.identifier.scopuseid_2-s2.0-79952725216en_HK
dc.identifier.hkuros186170en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79952725216&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume13en_HK
dc.identifier.issue13en_HK
dc.identifier.spage5888en_HK
dc.identifier.epage5896en_HK
dc.identifier.eissn1463-9084-
dc.identifier.isiWOS:000288447100047-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridXu, M=44161537500en_HK
dc.identifier.scopusauthoridSong, T=36087959100en_HK
dc.identifier.scopusauthoridQuan, Q=37018675200en_HK
dc.identifier.scopusauthoridHao, Q=35274915300en_HK
dc.identifier.scopusauthoridFang, DC=44160926500en_HK
dc.identifier.scopusauthoridSiu, CK=7006550712en_HK
dc.identifier.scopusauthoridChu, IK=7103327484en_HK

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