Identification of Modified Lysozyme Peptides upon Photo-oxidation by LC-TOF-MS
Protein oxidation can have major implications on the quality and safety of foods, but the majority of methods to evaluate oxidative damage lack specificity. Therefore, this study aimed to identify specific markers for protein oxidation. A well-characterized protein, lysozyme, was modified by photo-o...
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Veröffentlicht in: | Journal of agricultural and food chemistry 2013-12, Vol.61 (51), p.12727-12736 |
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container_title | Journal of agricultural and food chemistry |
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creator | Kerkaert, Barbara Mestdagh, Frédéric Obando, Monica Cucu, Tatiana De Meulenaer, Bruno |
description | Protein oxidation can have major implications on the quality and safety of foods, but the majority of methods to evaluate oxidative damage lack specificity. Therefore, this study aimed to identify specific markers for protein oxidation. A well-characterized protein, lysozyme, was modified by photo-oxidation and subsequently hydrolyzed prior to peptide analysis by LC-TOF-MS. A semiquantitative analysis of the peptides indicated that from the seven peptides containing sensitive amino acids, two peptides (HGLDNYR and WWCNDGR) were highly affected upon photo-oxidation and have the potential to serve as markers for protein oxidation. Site-specific modifications enabled the description of the degradation pathway of several lysozyme peptides but also indicated that the surrounding amino acids and the 3D structure of the protein have an impact on the induced modifications. It is therefore advisable to evaluate protein oxidation on the intact protein. |
doi_str_mv | 10.1021/jf404396c |
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Therefore, this study aimed to identify specific markers for protein oxidation. A well-characterized protein, lysozyme, was modified by photo-oxidation and subsequently hydrolyzed prior to peptide analysis by LC-TOF-MS. A semiquantitative analysis of the peptides indicated that from the seven peptides containing sensitive amino acids, two peptides (HGLDNYR and WWCNDGR) were highly affected upon photo-oxidation and have the potential to serve as markers for protein oxidation. Site-specific modifications enabled the description of the degradation pathway of several lysozyme peptides but also indicated that the surrounding amino acids and the 3D structure of the protein have an impact on the induced modifications. It is therefore advisable to evaluate protein oxidation on the intact protein.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf404396c</identifier><identifier>PMID: 24328178</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; amino acids ; Animals ; Biological and medical sciences ; Chickens ; Chromatography, High Pressure Liquid ; foods ; Fundamental and applied biological sciences. Psychology ; Light ; lysozyme ; Mass Spectrometry ; Molecular Sequence Data ; Muramidase - chemistry ; Muramidase - genetics ; Oxidation-Reduction - drug effects ; peptides ; Peptides - chemistry ; Peptides - genetics ; photooxidation ; protein structure</subject><ispartof>Journal of agricultural and food chemistry, 2013-12, Vol.61 (51), p.12727-12736</ispartof><rights>Copyright © 2013 American Chemical Society</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a369t-8c190c190aae2f7562e9425415da6b6509766bd5ed2856f963d763ec280963ec3</citedby><cites>FETCH-LOGICAL-a369t-8c190c190aae2f7562e9425415da6b6509766bd5ed2856f963d763ec280963ec3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf404396c$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf404396c$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2763,27075,27923,27924,56737,56787</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28079487$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24328178$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kerkaert, Barbara</creatorcontrib><creatorcontrib>Mestdagh, Frédéric</creatorcontrib><creatorcontrib>Obando, Monica</creatorcontrib><creatorcontrib>Cucu, Tatiana</creatorcontrib><creatorcontrib>De Meulenaer, Bruno</creatorcontrib><title>Identification of Modified Lysozyme Peptides upon Photo-oxidation by LC-TOF-MS</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Protein oxidation can have major implications on the quality and safety of foods, but the majority of methods to evaluate oxidative damage lack specificity. Therefore, this study aimed to identify specific markers for protein oxidation. A well-characterized protein, lysozyme, was modified by photo-oxidation and subsequently hydrolyzed prior to peptide analysis by LC-TOF-MS. A semiquantitative analysis of the peptides indicated that from the seven peptides containing sensitive amino acids, two peptides (HGLDNYR and WWCNDGR) were highly affected upon photo-oxidation and have the potential to serve as markers for protein oxidation. Site-specific modifications enabled the description of the degradation pathway of several lysozyme peptides but also indicated that the surrounding amino acids and the 3D structure of the protein have an impact on the induced modifications. It is therefore advisable to evaluate protein oxidation on the intact protein.</description><subject>Amino Acid Sequence</subject><subject>amino acids</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Chickens</subject><subject>Chromatography, High Pressure Liquid</subject><subject>foods</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Light</subject><subject>lysozyme</subject><subject>Mass Spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - genetics</subject><subject>Oxidation-Reduction - drug effects</subject><subject>peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>photooxidation</subject><subject>protein structure</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0MtKAzEUBuAgitbLwhfQ2Qi6GD3J5LqU4qVQL9B2PaS56JR2UiczYH16U1p14yIcQr78HH6ETjFcYyD4ZuYp0EJxs4N6mBHIGcZyF_UgPeaScXyADmOcAYBkAvbRAaEFkVjIHnoeWFe3la-MbqtQZ8FnT8Gmu7PZcBXD12rhsle3bCvrYtYtE3l9D23Iw2dlN1-mq2zYz8cv9_nT6BjteT2P7mQ7j9Dk_m7cf8yHLw-D_u0w1wVXbS4NVrA-WjviBePEKUoYxcxqPuUMlOB8apmzJK3vFS-s4IUzRIJaz-IIXW5yl0346Fxsy0UVjZvPde1CF0tMFQgqqGSJXm2oaUKMjfPlsqkWulmVGMp1feVvfcmebWO76cLZX_nTVwIXW6Cj0XPf6NpU8c9JEIpKkdz5xnkdSv3WJDMZEcAUAAuqWPGXpE0sZ6Fr6tTXPyt9A0NXimQ</recordid><startdate>20131226</startdate><enddate>20131226</enddate><creator>Kerkaert, Barbara</creator><creator>Mestdagh, Frédéric</creator><creator>Obando, Monica</creator><creator>Cucu, Tatiana</creator><creator>De Meulenaer, Bruno</creator><general>American Chemical Society</general><scope>FBQ</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></search><sort><creationdate>20131226</creationdate><title>Identification of Modified Lysozyme Peptides upon Photo-oxidation by LC-TOF-MS</title><author>Kerkaert, Barbara ; Mestdagh, Frédéric ; Obando, Monica ; Cucu, Tatiana ; De Meulenaer, Bruno</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a369t-8c190c190aae2f7562e9425415da6b6509766bd5ed2856f963d763ec280963ec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>amino acids</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Chickens</topic><topic>Chromatography, High Pressure Liquid</topic><topic>foods</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Light</topic><topic>lysozyme</topic><topic>Mass Spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Muramidase - chemistry</topic><topic>Muramidase - genetics</topic><topic>Oxidation-Reduction - drug effects</topic><topic>peptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - genetics</topic><topic>photooxidation</topic><topic>protein structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kerkaert, Barbara</creatorcontrib><creatorcontrib>Mestdagh, Frédéric</creatorcontrib><creatorcontrib>Obando, Monica</creatorcontrib><creatorcontrib>Cucu, Tatiana</creatorcontrib><creatorcontrib>De Meulenaer, Bruno</creatorcontrib><collection>AGRIS</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><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kerkaert, Barbara</au><au>Mestdagh, Frédéric</au><au>Obando, Monica</au><au>Cucu, Tatiana</au><au>De Meulenaer, Bruno</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of Modified Lysozyme Peptides upon Photo-oxidation by LC-TOF-MS</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2013-12-26</date><risdate>2013</risdate><volume>61</volume><issue>51</issue><spage>12727</spage><epage>12736</epage><pages>12727-12736</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Protein oxidation can have major implications on the quality and safety of foods, but the majority of methods to evaluate oxidative damage lack specificity. Therefore, this study aimed to identify specific markers for protein oxidation. A well-characterized protein, lysozyme, was modified by photo-oxidation and subsequently hydrolyzed prior to peptide analysis by LC-TOF-MS. A semiquantitative analysis of the peptides indicated that from the seven peptides containing sensitive amino acids, two peptides (HGLDNYR and WWCNDGR) were highly affected upon photo-oxidation and have the potential to serve as markers for protein oxidation. Site-specific modifications enabled the description of the degradation pathway of several lysozyme peptides but also indicated that the surrounding amino acids and the 3D structure of the protein have an impact on the induced modifications. It is therefore advisable to evaluate protein oxidation on the intact protein.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>24328178</pmid><doi>10.1021/jf404396c</doi><tpages>10</tpages></addata></record> |
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subjects | Amino Acid Sequence amino acids Animals Biological and medical sciences Chickens Chromatography, High Pressure Liquid foods Fundamental and applied biological sciences. Psychology Light lysozyme Mass Spectrometry Molecular Sequence Data Muramidase - chemistry Muramidase - genetics Oxidation-Reduction - drug effects peptides Peptides - chemistry Peptides - genetics photooxidation protein structure |
title | Identification of Modified Lysozyme Peptides upon Photo-oxidation by LC-TOF-MS |
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