Novel Cβ–Cγ Bond Cleavages of Tryptophan-Containing Peptide Radical Cations
In this study, we observed unprecedented cleavages of the C β –C γ bonds of tryptophan residue side chains in a series of hydrogen-deficient tryptophan-containing peptide radical cations (M •+ ) during low-energy collision-induced dissociation (CID). We used CID experiments and theoretical density f...
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creator | Song, Tao Hao, Qiang Law, Chun-Hin Siu, Chi-Kit Chu, Ivan K. |
description | In this study, we observed unprecedented cleavages of the C
β
–C
γ
bonds of tryptophan residue side chains in a series of hydrogen-deficient tryptophan-containing peptide radical cations (M
•+
) during low-energy collision-induced dissociation (CID). We used CID experiments and theoretical density functional theory (DFT) calculations to study the mechanism of this bond cleavage, which forms [M – 116]
+
ions. The formation of an α-carbon radical intermediate at the tryptophan residue for the subsequent C
β
–C
γ
bond cleavage is analogous to that occurring at leucine residues, producing the same product ions; this hypothesis was supported by the identical product ion spectra of [LGGGH – 43]
+
and [WGGGH – 116]
+
, obtained from the CID of [LGGGH]
•+
and [WGGGH]
•+
, respectively. Elimination of the neutral 116-Da radical requires inevitable dehydrogenation of the indole nitrogen atom, leaving the radical centered formally on the indole nitrogen atom ([Ind]
•
-2), in agreement with the CID data for [WGGGH]
•+
and [W
1-CH3
GGGH]
•+
; replacing the tryptophan residue with a 1-methyltryptophan residue results in a change of the base peak from that arising from a neutral radical loss (116 Da) to that arising from a molecule loss (131 Da), both originating from C
β
–C
γ
bond cleavage. Hydrogen atom transfer or proton transfer to the γ-carbon atom of the tryptophan residue weakens the C
β
–C
γ
bond and, therefore, decreases the dissociation energy barrier dramatically. |
doi_str_mv | 10.1007/s13361-011-0295-5 |
format | Article |
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β
–C
γ
bonds of tryptophan residue side chains in a series of hydrogen-deficient tryptophan-containing peptide radical cations (M
•+
) during low-energy collision-induced dissociation (CID). We used CID experiments and theoretical density functional theory (DFT) calculations to study the mechanism of this bond cleavage, which forms [M – 116]
+
ions. The formation of an α-carbon radical intermediate at the tryptophan residue for the subsequent C
β
–C
γ
bond cleavage is analogous to that occurring at leucine residues, producing the same product ions; this hypothesis was supported by the identical product ion spectra of [LGGGH – 43]
+
and [WGGGH – 116]
+
, obtained from the CID of [LGGGH]
•+
and [WGGGH]
•+
, respectively. Elimination of the neutral 116-Da radical requires inevitable dehydrogenation of the indole nitrogen atom, leaving the radical centered formally on the indole nitrogen atom ([Ind]
•
-2), in agreement with the CID data for [WGGGH]
•+
and [W
1-CH3
GGGH]
•+
; replacing the tryptophan residue with a 1-methyltryptophan residue results in a change of the base peak from that arising from a neutral radical loss (116 Da) to that arising from a molecule loss (131 Da), both originating from C
β
–C
γ
bond cleavage. Hydrogen atom transfer or proton transfer to the γ-carbon atom of the tryptophan residue weakens the C
β
–C
γ
bond and, therefore, decreases the dissociation energy barrier dramatically.</description><identifier>ISSN: 1044-0305</identifier><identifier>EISSN: 1879-1123</identifier><identifier>DOI: 10.1007/s13361-011-0295-5</identifier><identifier>PMID: 22135037</identifier><language>eng</language><publisher>New York: Springer-Verlag</publisher><subject>Aminoacids, peptides. Hormones. Neuropeptides ; Analytical Chemistry ; Analytical, structural and metabolic biochemistry ; Bioinformatics ; Biological and medical sciences ; Biotechnology ; Cations - chemistry ; Chemistry ; Chemistry and Materials Science ; Exact sciences and technology ; Free Radicals - chemistry ; Fundamental and applied biological sciences. Psychology ; Mass spectrometry ; Mass Spectrometry - methods ; Organic Chemistry ; Peptides - chemistry ; Proteins ; Proteomics ; Reactivity and mechanisms ; Research Article ; Tryptophan - chemistry</subject><ispartof>Journal of the American Society for Mass Spectrometry, 2012-02, Vol.23 (2), p.264-273</ispartof><rights>The Author(s) 2011</rights><rights>2015 INIST-CNRS</rights><rights>The Author(s) 2011. This article is published with open access at Springerlink.com</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c471t-621a29a53e9bcf38da2c6121b2be9b572ed72518f8ab40aa5bf62b9bf75650923</citedby><cites>FETCH-LOGICAL-c471t-621a29a53e9bcf38da2c6121b2be9b572ed72518f8ab40aa5bf62b9bf75650923</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s13361-011-0295-5$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s13361-011-0295-5$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25556402$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22135037$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Song, Tao</creatorcontrib><creatorcontrib>Hao, Qiang</creatorcontrib><creatorcontrib>Law, Chun-Hin</creatorcontrib><creatorcontrib>Siu, Chi-Kit</creatorcontrib><creatorcontrib>Chu, Ivan K.</creatorcontrib><title>Novel Cβ–Cγ Bond Cleavages of Tryptophan-Containing Peptide Radical Cations</title><title>Journal of the American Society for Mass Spectrometry</title><addtitle>J. Am. Soc. Mass Spectrom</addtitle><addtitle>J Am Soc Mass Spectrom</addtitle><description>In this study, we observed unprecedented cleavages of the C
β
–C
γ
bonds of tryptophan residue side chains in a series of hydrogen-deficient tryptophan-containing peptide radical cations (M
•+
) during low-energy collision-induced dissociation (CID). We used CID experiments and theoretical density functional theory (DFT) calculations to study the mechanism of this bond cleavage, which forms [M – 116]
+
ions. The formation of an α-carbon radical intermediate at the tryptophan residue for the subsequent C
β
–C
γ
bond cleavage is analogous to that occurring at leucine residues, producing the same product ions; this hypothesis was supported by the identical product ion spectra of [LGGGH – 43]
+
and [WGGGH – 116]
+
, obtained from the CID of [LGGGH]
•+
and [WGGGH]
•+
, respectively. Elimination of the neutral 116-Da radical requires inevitable dehydrogenation of the indole nitrogen atom, leaving the radical centered formally on the indole nitrogen atom ([Ind]
•
-2), in agreement with the CID data for [WGGGH]
•+
and [W
1-CH3
GGGH]
•+
; replacing the tryptophan residue with a 1-methyltryptophan residue results in a change of the base peak from that arising from a neutral radical loss (116 Da) to that arising from a molecule loss (131 Da), both originating from C
β
–C
γ
bond cleavage. Hydrogen atom transfer or proton transfer to the γ-carbon atom of the tryptophan residue weakens the C
β
–C
γ
bond and, therefore, decreases the dissociation energy barrier dramatically.</description><subject>Aminoacids, peptides. Hormones. Neuropeptides</subject><subject>Analytical Chemistry</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cations - chemistry</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Exact sciences and technology</subject><subject>Free Radicals - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Mass spectrometry</subject><subject>Mass Spectrometry - methods</subject><subject>Organic Chemistry</subject><subject>Peptides - chemistry</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Reactivity and mechanisms</subject><subject>Research Article</subject><subject>Tryptophan - chemistry</subject><issn>1044-0305</issn><issn>1879-1123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><recordid>eNp9kU9O3DAUxi1UxL_2AGyqbCpWAT87jpNNpRKVgoQAVdO19ZI4g1HGTu3MSOy4Q28C9-AQPQkezTDQTReWLb_f-z77fYQcAj0GSuVJAM5zSCnExUqRii2yB4UsUwDGP8QzzbKUcip2yX4Id5SCpKXcIbuMAReUyz1yfeUWuk-q58e_D3-q56fk1Nk2qXqNC5zqkLgumfj7YXTDLdq0cnZEY42dJjd6GE2rk5_YmgajAo7G2fCRbHfYB_1pvR-QX2ffJ9V5enn946L6dpk2mYQxzRkgK1FwXdZNx4sWWZMDg5rV8UZIplvJBBRdgXVGEUXd5awu606KXNCS8QPydaU7zOuZbhttR4-9GryZob9XDo36t2LNrZq6heIsz4ocosDRWsC733MdRjUzodF9j1a7eVAlyCJ6iSySsCIb70Lwutu4AFXLHNQqBxVzUMsclIg9n98_b9PxOvgIfFkDGOL4Oo-2MeGNE0LkGV3-k624EEt2qr26c3Nv42j_4_4CRFGi0Q</recordid><startdate>20120201</startdate><enddate>20120201</enddate><creator>Song, Tao</creator><creator>Hao, Qiang</creator><creator>Law, Chun-Hin</creator><creator>Siu, Chi-Kit</creator><creator>Chu, Ivan K.</creator><general>Springer-Verlag</general><general>Elsevier</general><scope>C6C</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20120201</creationdate><title>Novel Cβ–Cγ Bond Cleavages of Tryptophan-Containing Peptide Radical Cations</title><author>Song, Tao ; Hao, Qiang ; Law, Chun-Hin ; Siu, Chi-Kit ; Chu, Ivan K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c471t-621a29a53e9bcf38da2c6121b2be9b572ed72518f8ab40aa5bf62b9bf75650923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Aminoacids, peptides. Hormones. Neuropeptides</topic><topic>Analytical Chemistry</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cations - chemistry</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Exact sciences and technology</topic><topic>Free Radicals - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Mass spectrometry</topic><topic>Mass Spectrometry - methods</topic><topic>Organic Chemistry</topic><topic>Peptides - chemistry</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Reactivity and mechanisms</topic><topic>Research Article</topic><topic>Tryptophan - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Song, Tao</creatorcontrib><creatorcontrib>Hao, Qiang</creatorcontrib><creatorcontrib>Law, Chun-Hin</creatorcontrib><creatorcontrib>Siu, Chi-Kit</creatorcontrib><creatorcontrib>Chu, Ivan K.</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of the American Society for Mass Spectrometry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Song, Tao</au><au>Hao, Qiang</au><au>Law, Chun-Hin</au><au>Siu, Chi-Kit</au><au>Chu, Ivan K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel Cβ–Cγ Bond Cleavages of Tryptophan-Containing Peptide Radical Cations</atitle><jtitle>Journal of the American Society for Mass Spectrometry</jtitle><stitle>J. Am. Soc. Mass Spectrom</stitle><addtitle>J Am Soc Mass Spectrom</addtitle><date>2012-02-01</date><risdate>2012</risdate><volume>23</volume><issue>2</issue><spage>264</spage><epage>273</epage><pages>264-273</pages><issn>1044-0305</issn><eissn>1879-1123</eissn><abstract>In this study, we observed unprecedented cleavages of the C
β
–C
γ
bonds of tryptophan residue side chains in a series of hydrogen-deficient tryptophan-containing peptide radical cations (M
•+
) during low-energy collision-induced dissociation (CID). We used CID experiments and theoretical density functional theory (DFT) calculations to study the mechanism of this bond cleavage, which forms [M – 116]
+
ions. The formation of an α-carbon radical intermediate at the tryptophan residue for the subsequent C
β
–C
γ
bond cleavage is analogous to that occurring at leucine residues, producing the same product ions; this hypothesis was supported by the identical product ion spectra of [LGGGH – 43]
+
and [WGGGH – 116]
+
, obtained from the CID of [LGGGH]
•+
and [WGGGH]
•+
, respectively. Elimination of the neutral 116-Da radical requires inevitable dehydrogenation of the indole nitrogen atom, leaving the radical centered formally on the indole nitrogen atom ([Ind]
•
-2), in agreement with the CID data for [WGGGH]
•+
and [W
1-CH3
GGGH]
•+
; replacing the tryptophan residue with a 1-methyltryptophan residue results in a change of the base peak from that arising from a neutral radical loss (116 Da) to that arising from a molecule loss (131 Da), both originating from C
β
–C
γ
bond cleavage. Hydrogen atom transfer or proton transfer to the γ-carbon atom of the tryptophan residue weakens the C
β
–C
γ
bond and, therefore, decreases the dissociation energy barrier dramatically.</abstract><cop>New York</cop><pub>Springer-Verlag</pub><pmid>22135037</pmid><doi>10.1007/s13361-011-0295-5</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Aminoacids, peptides. Hormones. Neuropeptides Analytical Chemistry Analytical, structural and metabolic biochemistry Bioinformatics Biological and medical sciences Biotechnology Cations - chemistry Chemistry Chemistry and Materials Science Exact sciences and technology Free Radicals - chemistry Fundamental and applied biological sciences. Psychology Mass spectrometry Mass Spectrometry - methods Organic Chemistry Peptides - chemistry Proteins Proteomics Reactivity and mechanisms Research Article Tryptophan - chemistry |
title | Novel Cβ–Cγ Bond Cleavages of Tryptophan-Containing Peptide Radical Cations |
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