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Article: Effect of the basic residue on the energetics, dynamics, and mechanisms of gas-phase fragmentation of protonated peptides

TitleEffect of the basic residue on the energetics, dynamics, and mechanisms of gas-phase fragmentation of protonated peptides
Authors
Issue Date2010
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal Of The American Chemical Society, 2010, v. 132 n. 45, p. 16006-16016 How to Cite?
Abstract
The effect of the basic residue on the energetics, dynamics, and mechanisms of backbone fragmentation of protonated peptides was investigated. Time-resolved and collision energy-resolved surface-induced dissociation (SID) of singly protonated peptides with the N-terminal arginine residue and their analogues, in which arginine is replaced with less basic lysine and histidine residues, was examined using a specially configured Fourier transform ion cyclotron resonance mass spectrometer (FTICR-MS). SID experiments demonstrated different kinetics of formation of several primary product ions of peptides with and without arginine residue. The energetics and dynamics of these pathways were determined from Rice-Ramsperger-Kassel-Marcus (RRKM) modeling of the experimental data. Comparison between the kinetics and energetics of fragmentation of arginine-containing peptides and the corresponding methyl ester derivatives provides important information on the effect of dissociation pathways involving salt bridge (SB) intermediates on the observed fragmentation behavior. Because pathways involving SB intermediates are characterized by low threshold energies, they efficiently compete with classical oxazolone and imine/enol pathways of arginine-containing peptides on a long time scale of the FTICR instrument. In contrast, fragmentation of histidine- and lysine-containing peptides is largely determined by canonical pathways. Because SB pathways are characterized by negative activation entropies, fragmentation of arginine-containing peptides is kinetically hindered and observed at higher collision energies as compared to their lysine- and histidine-containing analogues. © 2010 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/135026
ISSN
2013 Impact Factor: 11.444
ISI Accession Number ID
Funding AgencyGrant Number
Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy (DOE)
University of Hong Kong and Hong Kong Research Grant Council, Special Administrative Region, China7012/08P
DOE's Office of Biological and Environmental Research
DOEDE-AC05-76RL01830
Funding Information:

This study was partially supported by the grant from the Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy (DOE), and the University of Hong Kong and Hong Kong Research Grant Council, Special Administrative Region, China (Project No. 7012/08P). The research described in this article was performed at the DOE's W.R. Wiley Environmental Molecular Sciences Laboratory (EMSL), a national scientific user facility sponsored by the DOE's Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory (PNNL). PNNL is operated by Battelle for the DOE under Contract DE-AC05-76RL01830.

References

 

Author Affiliations
  1. The University of Hong Kong
  2. Pacific Northwest National Laboratory
DC FieldValueLanguage
dc.contributor.authorLaskin, Jen_HK
dc.contributor.authorYang, Zen_HK
dc.contributor.authorSong, Ten_HK
dc.contributor.authorLam, Cen_HK
dc.contributor.authorChu, IKen_HK
dc.date.accessioned2011-07-27T01:26:14Z-
dc.date.available2011-07-27T01:26:14Z-
dc.date.issued2010en_HK
dc.identifier.citationJournal Of The American Chemical Society, 2010, v. 132 n. 45, p. 16006-16016en_HK
dc.identifier.issn0002-7863en_HK
dc.identifier.urihttp://hdl.handle.net/10722/135026-
dc.description.abstractThe effect of the basic residue on the energetics, dynamics, and mechanisms of backbone fragmentation of protonated peptides was investigated. Time-resolved and collision energy-resolved surface-induced dissociation (SID) of singly protonated peptides with the N-terminal arginine residue and their analogues, in which arginine is replaced with less basic lysine and histidine residues, was examined using a specially configured Fourier transform ion cyclotron resonance mass spectrometer (FTICR-MS). SID experiments demonstrated different kinetics of formation of several primary product ions of peptides with and without arginine residue. The energetics and dynamics of these pathways were determined from Rice-Ramsperger-Kassel-Marcus (RRKM) modeling of the experimental data. Comparison between the kinetics and energetics of fragmentation of arginine-containing peptides and the corresponding methyl ester derivatives provides important information on the effect of dissociation pathways involving salt bridge (SB) intermediates on the observed fragmentation behavior. Because pathways involving SB intermediates are characterized by low threshold energies, they efficiently compete with classical oxazolone and imine/enol pathways of arginine-containing peptides on a long time scale of the FTICR instrument. In contrast, fragmentation of histidine- and lysine-containing peptides is largely determined by canonical pathways. Because SB pathways are characterized by negative activation entropies, fragmentation of arginine-containing peptides is kinetically hindered and observed at higher collision energies as compared to their lysine- and histidine-containing analogues. © 2010 American Chemical Society.en_HK
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.htmlen_HK
dc.relation.ispartofJournal of the American Chemical Societyen_HK
dc.subject.meshArginine - chemistry-
dc.subject.meshEntropy-
dc.subject.meshGases - chemistry-
dc.subject.meshOligopeptides - chemistry-
dc.subject.meshPeptide Fragments - chemistry-
dc.titleEffect of the basic residue on the energetics, dynamics, and mechanisms of gas-phase fragmentation of protonated peptidesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0002-7863&volume=132&issue=45&spage=16006&epage=16016&date=2010&atitle=Effect+of+the+basic+residue+on+the+energetics,+dynamics,+and+mechanisms+of+gas-phase+fragmentation+of+protonated+peptidesen_US
dc.identifier.emailChu, IK:ivankchu@hku.hken_HK
dc.identifier.authorityChu, IK=rp00683en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/ja104438zen_HK
dc.identifier.pmid20977217en_HK
dc.identifier.scopuseid_2-s2.0-78449244153en_HK
dc.identifier.hkuros186187en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-78449244153&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume132en_HK
dc.identifier.issue45en_HK
dc.identifier.spage16006en_HK
dc.identifier.epage16016en_HK
dc.identifier.isiWOS:000284202200043-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLaskin, J=7102409836en_HK
dc.identifier.scopusauthoridYang, Z=36524476100en_HK
dc.identifier.scopusauthoridSong, T=36087959100en_HK
dc.identifier.scopusauthoridLam, C=7402990888en_HK
dc.identifier.scopusauthoridChu, IK=7103327484en_HK

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