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Article: The effect of the secondary structure on dissociation of peptide radical cations: Fragmentation of angiotensin III and its analogues

TitleThe effect of the secondary structure on dissociation of peptide radical cations: Fragmentation of angiotensin III and its analogues
Authors
Issue Date2008
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jpcbfk
Citation
Journal Of Physical Chemistry B, 2008, v. 112 n. 39, p. 12468-12478 How to Cite?
Abstract
Fragmentation of protonated RVYIHPF and RVYIHPF-OMe and the corresponding radical cations was studied using time- and collision energy-resolved surface-induced dissociation (SID) in a Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS) specially equipped to perform SID experiments. Peptide radical cations were produced by gas-phase fragmentation of CoIII(salen)-peptide complexes. Both the energetics and the mechanisms of dissociation of even-electron and odd-electron angiotensin III ions are quite different. Protonated molecules are much more stable toward fragmentation than the corresponding radical cations. RRKM modeling of the experimental data suggests that this stability is largely attributed to differences in threshold energies for dissociation, while activation entropies are very similar. Detailed analysis of the experimental data obtained for radical cations demonstrated the presence of two distinct structures separated by a high free-energy barrier. The two families of structures were ascribed to the canonical and zwitterionic forms of the radical cations produced in our experiments. © 2008 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/58413
ISSN
2013 Impact Factor: 3.377
2013 SCImago Journal Rankings: 1.575
ISI Accession Number ID
Funding AgencyGrant Number
Chemical Sciences Division, Office of Basic Energy Sciences of the U.S. DOE
University of Hong Kong
Hong Kong Research Grant Council
Special Administrative Region, China7018/06P
U.S. Department of Energy's Office of Biological and Environmental Research
Funding Information:

This study was partially supported by a grant from the Chemical Sciences Division, Office of Basic Energy Sciences of the U.S. DOE and partially by the University of Hong Kong and Hong Kong Research Grant Council, Special Administrative Region, China (Project No. 7018/06P). The research described in this Article 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. and C.L. acknowledge participation in the PNNL Interfacial and Condensed Phase Summer Research Institute. We thank Mr. Tao Song (University of Hong Kong) for stimulating discussions.

References

 

DC FieldValueLanguage
dc.contributor.authorYang, Zen_HK
dc.contributor.authorLam, Cen_HK
dc.contributor.authorChu, IKen_HK
dc.contributor.authorLaskin, Jen_HK
dc.date.accessioned2010-05-31T03:29:52Z-
dc.date.available2010-05-31T03:29:52Z-
dc.date.issued2008en_HK
dc.identifier.citationJournal Of Physical Chemistry B, 2008, v. 112 n. 39, p. 12468-12478en_HK
dc.identifier.issn1520-6106en_HK
dc.identifier.urihttp://hdl.handle.net/10722/58413-
dc.description.abstractFragmentation of protonated RVYIHPF and RVYIHPF-OMe and the corresponding radical cations was studied using time- and collision energy-resolved surface-induced dissociation (SID) in a Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS) specially equipped to perform SID experiments. Peptide radical cations were produced by gas-phase fragmentation of CoIII(salen)-peptide complexes. Both the energetics and the mechanisms of dissociation of even-electron and odd-electron angiotensin III ions are quite different. Protonated molecules are much more stable toward fragmentation than the corresponding radical cations. RRKM modeling of the experimental data suggests that this stability is largely attributed to differences in threshold energies for dissociation, while activation entropies are very similar. Detailed analysis of the experimental data obtained for radical cations demonstrated the presence of two distinct structures separated by a high free-energy barrier. The two families of structures were ascribed to the canonical and zwitterionic forms of the radical cations produced in our experiments. © 2008 American Chemical Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jpcbfken_HK
dc.relation.ispartofJournal of Physical Chemistry Ben_HK
dc.titleThe effect of the secondary structure on dissociation of peptide radical cations: Fragmentation of angiotensin III and its analoguesen_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.doi10.1021/jp805226xen_HK
dc.identifier.pmid18781717en_HK
dc.identifier.scopuseid_2-s2.0-54249102284en_HK
dc.identifier.hkuros155640en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-54249102284&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume112en_HK
dc.identifier.issue39en_HK
dc.identifier.spage12468en_HK
dc.identifier.epage12478en_HK
dc.identifier.isiWOS:000259552000040-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridYang, Z=36524476100en_HK
dc.identifier.scopusauthoridLam, C=7402990888en_HK
dc.identifier.scopusauthoridChu, IK=7103327484en_HK
dc.identifier.scopusauthoridLaskin, J=7102409836en_HK

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