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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Hauptverfasser: Hai-Tao Xia, Yu-Fen Liu, De-Fu Rong
Format: Tagungsbericht
Sprache:chi ; eng
Schlagworte:
Online-Zugang:Volltext bestellen
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 7163
container_issue
container_start_page 7161
container_title
container_volume
creator Hai-Tao Xia
Yu-Fen Liu
De-Fu Rong
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
fullrecord <record><control><sourceid>ieee_6IE</sourceid><recordid>TN_cdi_ieee_primary_5966017</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><ieee_id>5966017</ieee_id><sourcerecordid>5966017</sourcerecordid><originalsourceid>FETCH-LOGICAL-i90t-ba97a3d64d5fc7b44d018d0416a1b19ef066f8c16f2aa2edcc5b614582a6e6e63</originalsourceid><addsrcrecordid>eNo1kEFLw0AUhFdEUGv_gF72qIfEfZvNJnuUEq1QLNjeROrb7AtdadKy2ar99wasM4fhuwzDMHYNIgUQ5v51US2rVAqANDdaCyhO2CUoqZSBQmSnbGyK8p9lec7Gff8pBmlttFEX7GMR9-7Atx2Pa-K-ixSwjn5gS_GbqOMBA3HCENe83ra7Df3wtyrcTqCcSpnmL3Ku7uQ7x85xu_3yHfGewr7luLH71ndX7KzBTU_jY47Y8rFaTqbJbP70PHmYJd6ImFg0BWZOK5c3dWGVcgJKJxRoBAuGmmFwU9agG4koydV1bjWovJSoaXA2Yjd_tZ6IVrvgWwyH1fGT7Bc2vVST</addsrcrecordid><sourcetype>Publisher</sourcetype><iscdi>true</iscdi><recordtype>conference_proceeding</recordtype></control><display><type>conference_proceeding</type><title>Study on the interaction between rare earth complex [Er(C18H22.5N2O4)2] and bovine serum albumin</title><source>IEEE Electronic Library (IEL) Conference Proceedings</source><creator>Hai-Tao Xia ; Yu-Fen Liu ; De-Fu Rong</creator><creatorcontrib>Hai-Tao Xia ; Yu-Fen Liu ; De-Fu Rong</creatorcontrib><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><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>
fulltext fulltext_linktorsrc
identifier ISBN: 9781424491728
ispartof 2011 International Conference on Remote Sensing, Environment and Transportation Engineering, 2011, p.7161-7163
issn
language chi ; eng
recordid cdi_ieee_primary_5966017
source IEEE Electronic Library (IEL) Conference Proceedings
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-12T22%3A41%3A43IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-ieee_6IE&rft_val_fmt=info:ofi/fmt:kev:mtx:book&rft.genre=proceeding&rft.atitle=Study%20on%20the%20interaction%20between%20rare%20earth%20complex%20%5BEr(C18H22.5N2O4)2%5D%20and%20bovine%20serum%20albumin&rft.btitle=2011%20International%20Conference%20on%20Remote%20Sensing,%20Environment%20and%20Transportation%20Engineering&rft.au=Hai-Tao%20Xia&rft.date=2011-06&rft.spage=7161&rft.epage=7163&rft.pages=7161-7163&rft.isbn=9781424491728&rft.isbn_list=142449172X&rft_id=info:doi/10.1109/RSETE.2011.5966017&rft_dat=%3Cieee_6IE%3E5966017%3C/ieee_6IE%3E%3Curl%3E%3C/url%3E&rft.eisbn=1424491703&rft.eisbn_list=9781424491711&rft.eisbn_list=1424491711&rft.eisbn_list=9781424491704&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rft_ieee_id=5966017&rfr_iscdi=true