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Article: Electron Capture Dissociation of Peptides Metalated with Alkaline-Earth Metal Ions

TitleElectron Capture Dissociation of Peptides Metalated with Alkaline-Earth Metal Ions
Authors
Issue Date2006
Citation
Journal of the American Society for Mass Spectrometry, 2006, v. 17, n. 6, p. 757-771 How to Cite?
AbstractThe possible use of divalent alkaline-earth metal ions, including Mg 2+, Ca 2+, Sr 2+, and Ba 2+, as charge carrier for electron capture dissociation of peptides was investigated. Model peptides of RGGGVGGGR and NGGGWGGGN were used to simplify the interpretation of spectral information. It was demonstrated that useful electron capture dissociation (ECD) tandem mass spectra of these metalated peptides could be generated. Interestingly, peptides metalated with different alkaline-earth metal ions generated very similar ECD tandem mass spectra. Metalated c-ions and z-ions were the predominant fragment ions. Only Mg 2+-metalated peptides gave somewhat different results. Some nonmetalated c-ions were observed from ECD of [RGGGVGGGR + Mg] 2+ but not from [NGGGWGGGN + Mg] 2+. Together with some ab initio calculations, it was established that the bound metal ions might activate the acidity of the amide hydrogen. With the presence of high proton affinity moiety, such as N-terminal amino group and/or side chain of the arginine residues, the metalated peptide ions could exist predominantly in their zwitterion forms, in which one or two backbone amide group(s) was deprotonated and the high proton affinity functional group(s) was protonated. It was believed that electron capture leads primarily to the reduction of the mobile proton rather than the metal ions. With this zwitterion model, the formation of nonmetalated c-fragments and the generation of similar ECD spectra for peptides metalated with various alkaline-earth metal ions could readily to be explained. Another interesting observation in the ECD mass spectra of metalated peptides is related to the enhanced formation of the minor ECD products, i.e., (c - 1) +• and (z + 1) + ions. Together with ab initio calculations using a truncated peptide model, various possible reaction mechanisms for the formation of these minor ECD products were evaluated. It was concluded that hydrogen transfer between the initiated formed c and z · species plays an important role in the formation (c - 1) +• and (z + 1) + ions. Although peptides metalated with these metal ions do not have better ECD efficiency compared to the multiply-protonated peptides, it provides practical accessibility of ECD methods to analyze small peptides with no basic amino acid residues. © 2006 American Society for Mass Spectrometry.
Persistent Identifierhttp://hdl.handle.net/10722/206269
ISSN
2015 Impact Factor: 3.031
2015 SCImago Journal Rankings: 1.322
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorFung, Yi Man Eva-
dc.contributor.authorLiu, Haichuan-
dc.contributor.authorChan, Tak Wah Dominic-
dc.date.accessioned2014-10-22T01:25:32Z-
dc.date.available2014-10-22T01:25:32Z-
dc.date.issued2006-
dc.identifier.citationJournal of the American Society for Mass Spectrometry, 2006, v. 17, n. 6, p. 757-771-
dc.identifier.issn1044-0305-
dc.identifier.urihttp://hdl.handle.net/10722/206269-
dc.description.abstractThe possible use of divalent alkaline-earth metal ions, including Mg 2+, Ca 2+, Sr 2+, and Ba 2+, as charge carrier for electron capture dissociation of peptides was investigated. Model peptides of RGGGVGGGR and NGGGWGGGN were used to simplify the interpretation of spectral information. It was demonstrated that useful electron capture dissociation (ECD) tandem mass spectra of these metalated peptides could be generated. Interestingly, peptides metalated with different alkaline-earth metal ions generated very similar ECD tandem mass spectra. Metalated c-ions and z-ions were the predominant fragment ions. Only Mg 2+-metalated peptides gave somewhat different results. Some nonmetalated c-ions were observed from ECD of [RGGGVGGGR + Mg] 2+ but not from [NGGGWGGGN + Mg] 2+. Together with some ab initio calculations, it was established that the bound metal ions might activate the acidity of the amide hydrogen. With the presence of high proton affinity moiety, such as N-terminal amino group and/or side chain of the arginine residues, the metalated peptide ions could exist predominantly in their zwitterion forms, in which one or two backbone amide group(s) was deprotonated and the high proton affinity functional group(s) was protonated. It was believed that electron capture leads primarily to the reduction of the mobile proton rather than the metal ions. With this zwitterion model, the formation of nonmetalated c-fragments and the generation of similar ECD spectra for peptides metalated with various alkaline-earth metal ions could readily to be explained. Another interesting observation in the ECD mass spectra of metalated peptides is related to the enhanced formation of the minor ECD products, i.e., (c - 1) +• and (z + 1) + ions. Together with ab initio calculations using a truncated peptide model, various possible reaction mechanisms for the formation of these minor ECD products were evaluated. It was concluded that hydrogen transfer between the initiated formed c and z · species plays an important role in the formation (c - 1) +• and (z + 1) + ions. Although peptides metalated with these metal ions do not have better ECD efficiency compared to the multiply-protonated peptides, it provides practical accessibility of ECD methods to analyze small peptides with no basic amino acid residues. © 2006 American Society for Mass Spectrometry.-
dc.languageeng-
dc.relation.ispartofJournal of the American Society for Mass Spectrometry-
dc.titleElectron Capture Dissociation of Peptides Metalated with Alkaline-Earth Metal Ions-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jasms.2006.01.014-
dc.identifier.pmid16616861-
dc.identifier.scopuseid_2-s2.0-33646405722-
dc.identifier.volume17-
dc.identifier.issue6-
dc.identifier.spage757-
dc.identifier.epage771-
dc.identifier.isiWOS:000237913600002-

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