Water Dynamics in Egg White Peptide, Asp-His-Thr-Lys-Glu, Powder Monitored by Dynamic Vapor Sorption and LF-NMR
Water absorbed into the bulk amorphous structure of peptides can have profound effects on their properties. Here, we elucidated water dynamics in Asp-His-Thr-Lys-Glu (DHTKE), an antioxidant peptide derived from egg white ovalbumin, using water dynamic vapor sorption (DVS) and low-field nuclear magne...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2016-03, Vol.64 (10), p.2153-2161 |
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| container_issue | 10 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Yang, Shuailing Liu, Xuye Jin, Yan Li, Xingfang Chen, Feng Zhang, Mingdi Lin, Songyi |
| description | Water absorbed into the bulk amorphous structure of peptides can have profound effects on their properties. Here, we elucidated water dynamics in Asp-His-Thr-Lys-Glu (DHTKE), an antioxidant peptide derived from egg white ovalbumin, using water dynamic vapor sorption (DVS) and low-field nuclear magnetic resonance (LF-NMR). The DVS results indicated that parallel exponential kinetics model fitted well to the data of sorption kinetics behavior of DHTKE. Four different proton fractions with different mobilities were identified based on the degree of interaction between peptide and water. The water could significantly change the proton distribution and structure of the sample. The different phases of moisture absorption were reflected in the T 2 parameters. In addition, the combined water content was dominant in the hygroscopicity of DHTKE. This study provides an effective real-time monitoring method for water mobility and distribution in synthetic peptides, and this method may have applications in promoting peptide quality assurance. |
| doi_str_mv | 10.1021/acs.jafc.6b00056 |
| format | Article |
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Here, we elucidated water dynamics in Asp-His-Thr-Lys-Glu (DHTKE), an antioxidant peptide derived from egg white ovalbumin, using water dynamic vapor sorption (DVS) and low-field nuclear magnetic resonance (LF-NMR). The DVS results indicated that parallel exponential kinetics model fitted well to the data of sorption kinetics behavior of DHTKE. Four different proton fractions with different mobilities were identified based on the degree of interaction between peptide and water. The water could significantly change the proton distribution and structure of the sample. The different phases of moisture absorption were reflected in the T 2 parameters. In addition, the combined water content was dominant in the hygroscopicity of DHTKE. This study provides an effective real-time monitoring method for water mobility and distribution in synthetic peptides, and this method may have applications in promoting peptide quality assurance.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/acs.jafc.6b00056</identifier><identifier>PMID: 26915514</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Chickens ; Egg White - chemistry ; Kinetics ; Magnetic Resonance Spectroscopy - methods ; Peptides - chemistry ; Steam - analysis ; Water - chemistry</subject><ispartof>Journal of agricultural and food chemistry, 2016-03, Vol.64 (10), p.2153-2161</ispartof><rights>Copyright © 2016 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a336t-2bee931ca1c6e38a3d40e705a40a21c619b108f0f1efd2f9863c9040ba5925ab3</citedby><cites>FETCH-LOGICAL-a336t-2bee931ca1c6e38a3d40e705a40a21c619b108f0f1efd2f9863c9040ba5925ab3</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/acs.jafc.6b00056$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.jafc.6b00056$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2763,27075,27923,27924,56737,56787</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26915514$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Shuailing</creatorcontrib><creatorcontrib>Liu, Xuye</creatorcontrib><creatorcontrib>Jin, Yan</creatorcontrib><creatorcontrib>Li, Xingfang</creatorcontrib><creatorcontrib>Chen, Feng</creatorcontrib><creatorcontrib>Zhang, Mingdi</creatorcontrib><creatorcontrib>Lin, Songyi</creatorcontrib><title>Water Dynamics in Egg White Peptide, Asp-His-Thr-Lys-Glu, Powder Monitored by Dynamic Vapor Sorption and LF-NMR</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Water absorbed into the bulk amorphous structure of peptides can have profound effects on their properties. Here, we elucidated water dynamics in Asp-His-Thr-Lys-Glu (DHTKE), an antioxidant peptide derived from egg white ovalbumin, using water dynamic vapor sorption (DVS) and low-field nuclear magnetic resonance (LF-NMR). The DVS results indicated that parallel exponential kinetics model fitted well to the data of sorption kinetics behavior of DHTKE. Four different proton fractions with different mobilities were identified based on the degree of interaction between peptide and water. The water could significantly change the proton distribution and structure of the sample. The different phases of moisture absorption were reflected in the T 2 parameters. In addition, the combined water content was dominant in the hygroscopicity of DHTKE. This study provides an effective real-time monitoring method for water mobility and distribution in synthetic peptides, and this method may have applications in promoting peptide quality assurance.</description><subject>Animals</subject><subject>Chickens</subject><subject>Egg White - chemistry</subject><subject>Kinetics</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Peptides - chemistry</subject><subject>Steam - analysis</subject><subject>Water - chemistry</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM1PwjAYhxujEUTvnkyPHii-77aO7UiUDxNQoijHpds6GIF1tlvM_nuLgDdPTd48vyfpQ8gtQg_BwQeRmN5GZEnPjwGA-2ekjdwBxhGDc9IGy7CA-9giV8ZsLBLwPlySluOHyDl6baKWopKaPjWF2OWJoXlBh6sVXa7zStK5LKs8lV06MCWb5IYt1ppNG8PG27pL5-o7tdOZKvJKaZnSuDl56KcolabvSluBKqgoUjodsZfZ2zW5yMTWyJvj2yEfo-HiccKmr-Pnx8GUCdf1K-bEUoYuJgITX7qBcFMPZB-48EA49oZhjBBkkKHMUicLA99NQvAgFjx0uIjdDrk_eEutvmppqmiXm0Rut6KQqjYR9vse-h730KJwQBOtjNEyi0qd74RuIoRonzmymaN95uiY2U7ujvY63sn0b3DqaoHuAfidqloX9rP_-34AmtiHWQ</recordid><startdate>20160316</startdate><enddate>20160316</enddate><creator>Yang, Shuailing</creator><creator>Liu, Xuye</creator><creator>Jin, Yan</creator><creator>Li, Xingfang</creator><creator>Chen, Feng</creator><creator>Zhang, Mingdi</creator><creator>Lin, Songyi</creator><general>American Chemical Society</general><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>20160316</creationdate><title>Water Dynamics in Egg White Peptide, Asp-His-Thr-Lys-Glu, Powder Monitored by Dynamic Vapor Sorption and LF-NMR</title><author>Yang, Shuailing ; Liu, Xuye ; Jin, Yan ; Li, Xingfang ; Chen, Feng ; Zhang, Mingdi ; Lin, Songyi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a336t-2bee931ca1c6e38a3d40e705a40a21c619b108f0f1efd2f9863c9040ba5925ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animals</topic><topic>Chickens</topic><topic>Egg White - chemistry</topic><topic>Kinetics</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Peptides - chemistry</topic><topic>Steam - analysis</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Shuailing</creatorcontrib><creatorcontrib>Liu, Xuye</creatorcontrib><creatorcontrib>Jin, Yan</creatorcontrib><creatorcontrib>Li, Xingfang</creatorcontrib><creatorcontrib>Chen, Feng</creatorcontrib><creatorcontrib>Zhang, Mingdi</creatorcontrib><creatorcontrib>Lin, Songyi</creatorcontrib><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>Yang, Shuailing</au><au>Liu, Xuye</au><au>Jin, Yan</au><au>Li, Xingfang</au><au>Chen, Feng</au><au>Zhang, Mingdi</au><au>Lin, Songyi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Water Dynamics in Egg White Peptide, Asp-His-Thr-Lys-Glu, Powder Monitored by Dynamic Vapor Sorption and LF-NMR</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2016-03-16</date><risdate>2016</risdate><volume>64</volume><issue>10</issue><spage>2153</spage><epage>2161</epage><pages>2153-2161</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><abstract>Water absorbed into the bulk amorphous structure of peptides can have profound effects on their properties. Here, we elucidated water dynamics in Asp-His-Thr-Lys-Glu (DHTKE), an antioxidant peptide derived from egg white ovalbumin, using water dynamic vapor sorption (DVS) and low-field nuclear magnetic resonance (LF-NMR). The DVS results indicated that parallel exponential kinetics model fitted well to the data of sorption kinetics behavior of DHTKE. Four different proton fractions with different mobilities were identified based on the degree of interaction between peptide and water. The water could significantly change the proton distribution and structure of the sample. The different phases of moisture absorption were reflected in the T 2 parameters. In addition, the combined water content was dominant in the hygroscopicity of DHTKE. This study provides an effective real-time monitoring method for water mobility and distribution in synthetic peptides, and this method may have applications in promoting peptide quality assurance.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>26915514</pmid><doi>10.1021/acs.jafc.6b00056</doi><tpages>9</tpages></addata></record> |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Animals Chickens Egg White - chemistry Kinetics Magnetic Resonance Spectroscopy - methods Peptides - chemistry Steam - analysis Water - chemistry |
| title | Water Dynamics in Egg White Peptide, Asp-His-Thr-Lys-Glu, Powder Monitored by Dynamic Vapor Sorption and LF-NMR |
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