Characterization of the binding of chrysoidine, an illegal food additive to bovine serum albumin
•The binding stoichiometry of chrysoidine to BSA is 1:15.5.•Sudlow site I in domain IIA is identified as the most possible binding site.•Van der Waals and hydrogen bonding interactions play a major role in the binding.•No detectable conformational change of BSA is observed during the binding process...
Gespeichert in:
| Veröffentlicht in: | Food and chemical toxicology 2014-03, Vol.65, p.227-232 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 232 |
|---|---|
| container_issue | |
| container_start_page | 227 |
| container_title | Food and chemical toxicology |
| container_volume | 65 |
| creator | Yang, Bingjun Hao, Fang Li, Jiarong Wei, Kai Wang, Wenyu Liu, Rutao |
| description | •The binding stoichiometry of chrysoidine to BSA is 1:15.5.•Sudlow site I in domain IIA is identified as the most possible binding site.•Van der Waals and hydrogen bonding interactions play a major role in the binding.•No detectable conformational change of BSA is observed during the binding process.•Förster resonance energy transfer occurred between BSA and chrysoidine.
Chrysoidine is an industrial azo dye and the presence of chrysoidine in water and food has become an environmental concern due to its negative effects on human beings. Binding of dyes to serum albumins significantly influence their absorption, distribution, metabolism, and excretion properties. In this work, the interactions of chrysoidine with bovine serum albumin (BSA) were explored. Isothermal titration calorimetry results reveal the binding stoichiometry of chrysoidine to BSA is 1:15.5, and van der Waals and hydrogen bonding interactions are the major driving force in the binding of chrysoidine to BSA. Molecular docking simulations show that chrysoidine binds to BSA at a cavity close to Sudlow site I in domain IIA. However, no detectable conformational change of BSA occurs in the presence of chrysoidine as revealed by UV–vis absorption, circular dichroism and fluorescence spectroscopy studies. |
| doi_str_mv | 10.1016/j.fct.2013.12.047 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1647023192</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0278691513008697</els_id><sourcerecordid>1647023192</sourcerecordid><originalsourceid>FETCH-LOGICAL-c416t-31cf52a03e9386f298d86e0adc27e748c53da306ae07f9410fb792cf6abd301d3</originalsourceid><addsrcrecordid>eNp9kE1v1DAQhi1ERZfCD-CCfEHiQIK_YsfiVK34qFSpFzgbxx53vUriYicrlV9fr3aBG6fRSM_7zuhB6A0lLSVUfty3wS0tI5S3lLVEqGdoQ3vFG8k7-hxtCFN9IzXtLtHLUvaEEEWVfIEumeBaiF5u0M_tzmbrFsjxt11imnEKeNkBHuLs43x_XN0uP5YU6wofsJ1xHEe4tyMOKXlsvY9LPABeEh7SoTK4QF4nbMdhneL8Cl0EOxZ4fZ5X6MeXz9-335rbu6832-vbxgkql4ZTFzpmCQfNexmY7n0vgVjvmAIletdxbzmRFogKWlASBqWZC9IOnhPq-RV6f-p9yOnXCmUxUywOxtHOkNZiqBSKME41qyg9oS6nUjIE85DjZPOjocQcxZq9qWLNUayhzFSxNfP2XL8OE_i_iT8mK_DuDNji7BiynV0s_7iek05rUblPJw6qjEOEbIqLMDvwMUM96lP8zxtPH0yWSA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1647023192</pqid></control><display><type>article</type><title>Characterization of the binding of chrysoidine, an illegal food additive to bovine serum albumin</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Yang, Bingjun ; Hao, Fang ; Li, Jiarong ; Wei, Kai ; Wang, Wenyu ; Liu, Rutao</creator><creatorcontrib>Yang, Bingjun ; Hao, Fang ; Li, Jiarong ; Wei, Kai ; Wang, Wenyu ; Liu, Rutao</creatorcontrib><description>•The binding stoichiometry of chrysoidine to BSA is 1:15.5.•Sudlow site I in domain IIA is identified as the most possible binding site.•Van der Waals and hydrogen bonding interactions play a major role in the binding.•No detectable conformational change of BSA is observed during the binding process.•Förster resonance energy transfer occurred between BSA and chrysoidine.
Chrysoidine is an industrial azo dye and the presence of chrysoidine in water and food has become an environmental concern due to its negative effects on human beings. Binding of dyes to serum albumins significantly influence their absorption, distribution, metabolism, and excretion properties. In this work, the interactions of chrysoidine with bovine serum albumin (BSA) were explored. Isothermal titration calorimetry results reveal the binding stoichiometry of chrysoidine to BSA is 1:15.5, and van der Waals and hydrogen bonding interactions are the major driving force in the binding of chrysoidine to BSA. Molecular docking simulations show that chrysoidine binds to BSA at a cavity close to Sudlow site I in domain IIA. However, no detectable conformational change of BSA occurs in the presence of chrysoidine as revealed by UV–vis absorption, circular dichroism and fluorescence spectroscopy studies.</description><identifier>ISSN: 0278-6915</identifier><identifier>EISSN: 1873-6351</identifier><identifier>DOI: 10.1016/j.fct.2013.12.047</identifier><identifier>PMID: 24394486</identifier><identifier>CODEN: FCTOD7</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Biological and medical sciences ; Circular Dichroism ; Dyes ; Food Additives - metabolism ; Isothermal titration calorimetry ; Medical sciences ; Molecular docking ; Molecular Docking Simulation ; p-Aminoazobenzene - analogs & derivatives ; p-Aminoazobenzene - metabolism ; Protein Binding ; Proteins ; Serum Albumin, Bovine - metabolism ; Spectrometry, Fluorescence ; Spectrophotometry, Ultraviolet ; Spectroscopy ; Thermodynamics ; Toxicology</subject><ispartof>Food and chemical toxicology, 2014-03, Vol.65, p.227-232</ispartof><rights>2014 Elsevier Ltd</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2014 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c416t-31cf52a03e9386f298d86e0adc27e748c53da306ae07f9410fb792cf6abd301d3</citedby><cites>FETCH-LOGICAL-c416t-31cf52a03e9386f298d86e0adc27e748c53da306ae07f9410fb792cf6abd301d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0278691513008697$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28305994$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24394486$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Bingjun</creatorcontrib><creatorcontrib>Hao, Fang</creatorcontrib><creatorcontrib>Li, Jiarong</creatorcontrib><creatorcontrib>Wei, Kai</creatorcontrib><creatorcontrib>Wang, Wenyu</creatorcontrib><creatorcontrib>Liu, Rutao</creatorcontrib><title>Characterization of the binding of chrysoidine, an illegal food additive to bovine serum albumin</title><title>Food and chemical toxicology</title><addtitle>Food Chem Toxicol</addtitle><description>•The binding stoichiometry of chrysoidine to BSA is 1:15.5.•Sudlow site I in domain IIA is identified as the most possible binding site.•Van der Waals and hydrogen bonding interactions play a major role in the binding.•No detectable conformational change of BSA is observed during the binding process.•Förster resonance energy transfer occurred between BSA and chrysoidine.
Chrysoidine is an industrial azo dye and the presence of chrysoidine in water and food has become an environmental concern due to its negative effects on human beings. Binding of dyes to serum albumins significantly influence their absorption, distribution, metabolism, and excretion properties. In this work, the interactions of chrysoidine with bovine serum albumin (BSA) were explored. Isothermal titration calorimetry results reveal the binding stoichiometry of chrysoidine to BSA is 1:15.5, and van der Waals and hydrogen bonding interactions are the major driving force in the binding of chrysoidine to BSA. Molecular docking simulations show that chrysoidine binds to BSA at a cavity close to Sudlow site I in domain IIA. However, no detectable conformational change of BSA occurs in the presence of chrysoidine as revealed by UV–vis absorption, circular dichroism and fluorescence spectroscopy studies.</description><subject>Biological and medical sciences</subject><subject>Circular Dichroism</subject><subject>Dyes</subject><subject>Food Additives - metabolism</subject><subject>Isothermal titration calorimetry</subject><subject>Medical sciences</subject><subject>Molecular docking</subject><subject>Molecular Docking Simulation</subject><subject>p-Aminoazobenzene - analogs & derivatives</subject><subject>p-Aminoazobenzene - metabolism</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Serum Albumin, Bovine - metabolism</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Spectroscopy</subject><subject>Thermodynamics</subject><subject>Toxicology</subject><issn>0278-6915</issn><issn>1873-6351</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1v1DAQhi1ERZfCD-CCfEHiQIK_YsfiVK34qFSpFzgbxx53vUriYicrlV9fr3aBG6fRSM_7zuhB6A0lLSVUfty3wS0tI5S3lLVEqGdoQ3vFG8k7-hxtCFN9IzXtLtHLUvaEEEWVfIEumeBaiF5u0M_tzmbrFsjxt11imnEKeNkBHuLs43x_XN0uP5YU6wofsJ1xHEe4tyMOKXlsvY9LPABeEh7SoTK4QF4nbMdhneL8Cl0EOxZ4fZ5X6MeXz9-335rbu6832-vbxgkql4ZTFzpmCQfNexmY7n0vgVjvmAIletdxbzmRFogKWlASBqWZC9IOnhPq-RV6f-p9yOnXCmUxUywOxtHOkNZiqBSKME41qyg9oS6nUjIE85DjZPOjocQcxZq9qWLNUayhzFSxNfP2XL8OE_i_iT8mK_DuDNji7BiynV0s_7iek05rUblPJw6qjEOEbIqLMDvwMUM96lP8zxtPH0yWSA</recordid><startdate>20140301</startdate><enddate>20140301</enddate><creator>Yang, Bingjun</creator><creator>Hao, Fang</creator><creator>Li, Jiarong</creator><creator>Wei, Kai</creator><creator>Wang, Wenyu</creator><creator>Liu, Rutao</creator><general>Elsevier Ltd</general><general>Elsevier</general><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>7U7</scope><scope>C1K</scope></search><sort><creationdate>20140301</creationdate><title>Characterization of the binding of chrysoidine, an illegal food additive to bovine serum albumin</title><author>Yang, Bingjun ; Hao, Fang ; Li, Jiarong ; Wei, Kai ; Wang, Wenyu ; Liu, Rutao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c416t-31cf52a03e9386f298d86e0adc27e748c53da306ae07f9410fb792cf6abd301d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Biological and medical sciences</topic><topic>Circular Dichroism</topic><topic>Dyes</topic><topic>Food Additives - metabolism</topic><topic>Isothermal titration calorimetry</topic><topic>Medical sciences</topic><topic>Molecular docking</topic><topic>Molecular Docking Simulation</topic><topic>p-Aminoazobenzene - analogs & derivatives</topic><topic>p-Aminoazobenzene - metabolism</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Serum Albumin, Bovine - metabolism</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Spectroscopy</topic><topic>Thermodynamics</topic><topic>Toxicology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Bingjun</creatorcontrib><creatorcontrib>Hao, Fang</creatorcontrib><creatorcontrib>Li, Jiarong</creatorcontrib><creatorcontrib>Wei, Kai</creatorcontrib><creatorcontrib>Wang, Wenyu</creatorcontrib><creatorcontrib>Liu, Rutao</creatorcontrib><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>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Food and chemical toxicology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Bingjun</au><au>Hao, Fang</au><au>Li, Jiarong</au><au>Wei, Kai</au><au>Wang, Wenyu</au><au>Liu, Rutao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the binding of chrysoidine, an illegal food additive to bovine serum albumin</atitle><jtitle>Food and chemical toxicology</jtitle><addtitle>Food Chem Toxicol</addtitle><date>2014-03-01</date><risdate>2014</risdate><volume>65</volume><spage>227</spage><epage>232</epage><pages>227-232</pages><issn>0278-6915</issn><eissn>1873-6351</eissn><coden>FCTOD7</coden><abstract>•The binding stoichiometry of chrysoidine to BSA is 1:15.5.•Sudlow site I in domain IIA is identified as the most possible binding site.•Van der Waals and hydrogen bonding interactions play a major role in the binding.•No detectable conformational change of BSA is observed during the binding process.•Förster resonance energy transfer occurred between BSA and chrysoidine.
Chrysoidine is an industrial azo dye and the presence of chrysoidine in water and food has become an environmental concern due to its negative effects on human beings. Binding of dyes to serum albumins significantly influence their absorption, distribution, metabolism, and excretion properties. In this work, the interactions of chrysoidine with bovine serum albumin (BSA) were explored. Isothermal titration calorimetry results reveal the binding stoichiometry of chrysoidine to BSA is 1:15.5, and van der Waals and hydrogen bonding interactions are the major driving force in the binding of chrysoidine to BSA. Molecular docking simulations show that chrysoidine binds to BSA at a cavity close to Sudlow site I in domain IIA. However, no detectable conformational change of BSA occurs in the presence of chrysoidine as revealed by UV–vis absorption, circular dichroism and fluorescence spectroscopy studies.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>24394486</pmid><doi>10.1016/j.fct.2013.12.047</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0278-6915 |
| ispartof | Food and chemical toxicology, 2014-03, Vol.65, p.227-232 |
| issn | 0278-6915 1873-6351 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1647023192 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Biological and medical sciences Circular Dichroism Dyes Food Additives - metabolism Isothermal titration calorimetry Medical sciences Molecular docking Molecular Docking Simulation p-Aminoazobenzene - analogs & derivatives p-Aminoazobenzene - metabolism Protein Binding Proteins Serum Albumin, Bovine - metabolism Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Spectroscopy Thermodynamics Toxicology |
| title | Characterization of the binding of chrysoidine, an illegal food additive to bovine serum albumin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-07T18%3A28%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterization%20of%20the%20binding%20of%20chrysoidine,%20an%20illegal%20food%20additive%20to%20bovine%20serum%20albumin&rft.jtitle=Food%20and%20chemical%20toxicology&rft.au=Yang,%20Bingjun&rft.date=2014-03-01&rft.volume=65&rft.spage=227&rft.epage=232&rft.pages=227-232&rft.issn=0278-6915&rft.eissn=1873-6351&rft.coden=FCTOD7&rft_id=info:doi/10.1016/j.fct.2013.12.047&rft_dat=%3Cproquest_cross%3E1647023192%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1647023192&rft_id=info:pmid/24394486&rft_els_id=S0278691513008697&rfr_iscdi=true |