Linked Life Data

17126025

Source:http://linkedlifedata.com/resource/pubmed/id/17126025

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-2-23
pubmed:abstractText
Thio-ether bonds in the cysteinyl side chain of peptides, formed with the most commonly used cysteine blocking reagent iodoacetamide, after conversion to sulfoxide, releases a neutral fragment mass in a low-energy MS/MS experiment in the gas phase of the mass spectrometer [6]. In this study, we show that the neutral loss fragments produced from the mono-oxidized thio-ether bonds (sulfoxide) in peptides, formed by alkyl halide or double-bond containing cysteine blocking reagents are different under low-energy MS/MS conditions. We have evaluated the low-energy fragmentation patterns of mono-oxidized modified peptides with different cysteine blocking reagents, such as iodoacetamide, 3-maleimidopropionic acid, and 4-vinylpyridine using FTICR-MS. We propose that the mechanisms of gas-phase fragmentation of mono-oxidized thio-ether bonds in the side chain of peptides, formed by iodoacetamide and double-bond containing cysteine blocking reagents, maleimide and vinylpyridine, are different because of the availability of acidic beta-hydrogens in these compounds. Moreover, we investigated the fragmentation characteristics of mono-oxidized thio-ether bonds within the peptide sequence to develop novel mass-spectrometry identifiable chemical cross-linkers. This methionine type of oxidized thio-ether bond within the peptide sequence did not show anticipated low-energy fragmentation. Electron capture dissociation (ECD) of the side chain thio-ether bond containing oxidized peptides was also studied. ECD spectra of the oxidized peptides showed a greater extent of peptide backbone cleavage, compared with CID spectra. This fragmentation information is critical to researchers for accurate data analysis of this undesired modification in proteomics research, as well as other methods that may utilize sulfoxide derivatives.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-11212008, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-12216740, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-12781462, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-15359728, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-15389855, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-15450492, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-15623310, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-16023363, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-16512663, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-5131162, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-6528972, http://linkedlifedata.com/resource/pubmed/commentcorrection/17126025-9868912
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1044-0305
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
493-501
pubmed:dateRevised
2011-5-30
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Evaluation of low energy CID and ECD fragmentation behavior of mono-oxidized thio-ether bonds in peptides.
pubmed:affiliation
Department of Chemistry, Washington State University, Pullman, Washington 99164-4630, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't