Study on the interaction between rare earth complex [Er(C18H22.5N2O4)2] and bovine serum albumin
The interaction of rare earth complex [Er(C 18 H 22.5 N 2 O 4 ) 2 ] and bovine serum albumin (BSA) under physiological condition was studied by fluorescence spectrum. The experiment demonstrated that the fluorescence quenching of BSA by Er(III) complex is a result of the formation of ground state co...
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description | The interaction of rare earth complex [Er(C 18 H 22.5 N 2 O 4 ) 2 ] and bovine serum albumin (BSA) under physiological condition was studied by fluorescence spectrum. The experiment demonstrated that the fluorescence quenching of BSA by Er(III) complex is a result of the formation of ground state complex and the quenching mechanism is mainly static quenching. The corresponding binding constants between Er(III) complex and BSA were 5.17×10 3 L.mol -1 (293K), and the binding sites were 1. According to the binding constants of the different temperatures, the thermodynamic parameters AH, AG, AS were calculated. From thermodynamic parameters it can be judged that the binding force between Er(III) complex and BSA is mainly H-bond and Van der Waals force. The effect of Er(III) complex on the conformation of BSA was analyzed by synchronous fluorescence spectrometry. |
doi_str_mv | 10.1109/RSETE.2011.5966017 |
format | Conference Proceeding |
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The experiment demonstrated that the fluorescence quenching of BSA by Er(III) complex is a result of the formation of ground state complex and the quenching mechanism is mainly static quenching. The corresponding binding constants between Er(III) complex and BSA were 5.17×10 3 L.mol -1 (293K), and the binding sites were 1. According to the binding constants of the different temperatures, the thermodynamic parameters AH, AG, AS were calculated. From thermodynamic parameters it can be judged that the binding force between Er(III) complex and BSA is mainly H-bond and Van der Waals force. The effect of Er(III) complex on the conformation of BSA was analyzed by synchronous fluorescence spectrometry.</description><identifier>ISBN: 9781424491728</identifier><identifier>ISBN: 142449172X</identifier><identifier>EISBN: 1424491703</identifier><identifier>EISBN: 9781424491711</identifier><identifier>EISBN: 1424491711</identifier><identifier>EISBN: 9781424491704</identifier><identifier>DOI: 10.1109/RSETE.2011.5966017</identifier><language>chi ; eng</language><publisher>IEEE</publisher><subject>Biochemistry ; Bovine ; Bovine serum albumin ; Fluorescence ; Fluorescence spectrum ; Force ; Land surface temperature ; Rare earth complex ; Spectroscopy ; Thermodynamics</subject><ispartof>2011 International Conference on Remote Sensing, Environment and Transportation Engineering, 2011, p.7161-7163</ispartof><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://ieeexplore.ieee.org/document/5966017$$EHTML$$P50$$Gieee$$H</linktohtml><link.rule.ids>309,310,776,780,785,786,2052,27902,54895</link.rule.ids><linktorsrc>$$Uhttps://ieeexplore.ieee.org/document/5966017$$EView_record_in_IEEE$$FView_record_in_$$GIEEE</linktorsrc></links><search><creatorcontrib>Hai-Tao Xia</creatorcontrib><creatorcontrib>Yu-Fen Liu</creatorcontrib><creatorcontrib>De-Fu Rong</creatorcontrib><title>Study on the interaction between rare earth complex [Er(C18H22.5N2O4)2] and bovine serum albumin</title><title>2011 International Conference on Remote Sensing, Environment and Transportation Engineering</title><addtitle>RSETE</addtitle><description>The interaction of rare earth complex [Er(C 18 H 22.5 N 2 O 4 ) 2 ] and bovine serum albumin (BSA) under physiological condition was studied by fluorescence spectrum. The experiment demonstrated that the fluorescence quenching of BSA by Er(III) complex is a result of the formation of ground state complex and the quenching mechanism is mainly static quenching. The corresponding binding constants between Er(III) complex and BSA were 5.17×10 3 L.mol -1 (293K), and the binding sites were 1. According to the binding constants of the different temperatures, the thermodynamic parameters AH, AG, AS were calculated. From thermodynamic parameters it can be judged that the binding force between Er(III) complex and BSA is mainly H-bond and Van der Waals force. The effect of Er(III) complex on the conformation of BSA was analyzed by synchronous fluorescence spectrometry.</description><subject>Biochemistry</subject><subject>Bovine</subject><subject>Bovine serum albumin</subject><subject>Fluorescence</subject><subject>Fluorescence spectrum</subject><subject>Force</subject><subject>Land surface temperature</subject><subject>Rare earth complex</subject><subject>Spectroscopy</subject><subject>Thermodynamics</subject><isbn>9781424491728</isbn><isbn>142449172X</isbn><isbn>1424491703</isbn><isbn>9781424491711</isbn><isbn>1424491711</isbn><isbn>9781424491704</isbn><fulltext>true</fulltext><rsrctype>conference_proceeding</rsrctype><creationdate>2011</creationdate><recordtype>conference_proceeding</recordtype><sourceid>6IE</sourceid><sourceid>RIE</sourceid><recordid>eNo1kEFLw0AUhFdEUGv_gF72qIfEfZvNJnuUEq1QLNjeROrb7AtdadKy2ar99wasM4fhuwzDMHYNIgUQ5v51US2rVAqANDdaCyhO2CUoqZSBQmSnbGyK8p9lec7Gff8pBmlttFEX7GMR9-7Atx2Pa-K-ixSwjn5gS_GbqOMBA3HCENe83ra7Df3wtyrcTqCcSpnmL3Ku7uQ7x85xu_3yHfGewr7luLH71ndX7KzBTU_jY47Y8rFaTqbJbP70PHmYJd6ImFg0BWZOK5c3dWGVcgJKJxRoBAuGmmFwU9agG4koydV1bjWovJSoaXA2Yjd_tZ6IVrvgWwyH1fGT7Bc2vVST</recordid><startdate>201106</startdate><enddate>201106</enddate><creator>Hai-Tao Xia</creator><creator>Yu-Fen Liu</creator><creator>De-Fu Rong</creator><general>IEEE</general><scope>6IE</scope><scope>6IL</scope><scope>CBEJK</scope><scope>RIE</scope><scope>RIL</scope></search><sort><creationdate>201106</creationdate><title>Study on the interaction between rare earth complex [Er(C18H22.5N2O4)2] and bovine serum albumin</title><author>Hai-Tao Xia ; Yu-Fen Liu ; De-Fu Rong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i90t-ba97a3d64d5fc7b44d018d0416a1b19ef066f8c16f2aa2edcc5b614582a6e6e63</frbrgroupid><rsrctype>conference_proceedings</rsrctype><prefilter>conference_proceedings</prefilter><language>chi ; eng</language><creationdate>2011</creationdate><topic>Biochemistry</topic><topic>Bovine</topic><topic>Bovine serum albumin</topic><topic>Fluorescence</topic><topic>Fluorescence spectrum</topic><topic>Force</topic><topic>Land surface temperature</topic><topic>Rare earth complex</topic><topic>Spectroscopy</topic><topic>Thermodynamics</topic><toplevel>online_resources</toplevel><creatorcontrib>Hai-Tao Xia</creatorcontrib><creatorcontrib>Yu-Fen Liu</creatorcontrib><creatorcontrib>De-Fu Rong</creatorcontrib><collection>IEEE Electronic Library (IEL) Conference Proceedings</collection><collection>IEEE Proceedings Order Plan All Online (POP All Online) 1998-present by volume</collection><collection>IEEE Xplore All Conference Proceedings</collection><collection>IEEE Electronic Library (IEL)</collection><collection>IEEE Proceedings Order Plans (POP All) 1998-Present</collection></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Hai-Tao Xia</au><au>Yu-Fen Liu</au><au>De-Fu Rong</au><format>book</format><genre>proceeding</genre><ristype>CONF</ristype><atitle>Study on the interaction between rare earth complex [Er(C18H22.5N2O4)2] and bovine serum albumin</atitle><btitle>2011 International Conference on Remote Sensing, Environment and Transportation Engineering</btitle><stitle>RSETE</stitle><date>2011-06</date><risdate>2011</risdate><spage>7161</spage><epage>7163</epage><pages>7161-7163</pages><isbn>9781424491728</isbn><isbn>142449172X</isbn><eisbn>1424491703</eisbn><eisbn>9781424491711</eisbn><eisbn>1424491711</eisbn><eisbn>9781424491704</eisbn><abstract>The interaction of rare earth complex [Er(C 18 H 22.5 N 2 O 4 ) 2 ] and bovine serum albumin (BSA) under physiological condition was studied by fluorescence spectrum. The experiment demonstrated that the fluorescence quenching of BSA by Er(III) complex is a result of the formation of ground state complex and the quenching mechanism is mainly static quenching. The corresponding binding constants between Er(III) complex and BSA were 5.17×10 3 L.mol -1 (293K), and the binding sites were 1. According to the binding constants of the different temperatures, the thermodynamic parameters AH, AG, AS were calculated. From thermodynamic parameters it can be judged that the binding force between Er(III) complex and BSA is mainly H-bond and Van der Waals force. The effect of Er(III) complex on the conformation of BSA was analyzed by synchronous fluorescence spectrometry.</abstract><pub>IEEE</pub><doi>10.1109/RSETE.2011.5966017</doi><tpages>3</tpages></addata></record> |
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subjects | Biochemistry Bovine Bovine serum albumin Fluorescence Fluorescence spectrum Force Land surface temperature Rare earth complex Spectroscopy Thermodynamics |
title | Study on the interaction between rare earth complex [Er(C18H22.5N2O4)2] and bovine serum albumin |
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