Classification of the Binding Modes in Bovine Serum Albumin Using Terminally Substituted Alkane Analogues
With the fluorescence probe of 8-anilino-1-naphthalenesulfonate (ANS), the binding modes of terminally substituted alkane analogues (CnX; X = COOH, OH, CHO, NH3, CONH2) to bovine serum albumin (BSA) were investigated using a competitive binding technique. The Scatchard plot of the fluorometric titra...
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| Veröffentlicht in: | Analytical Sciences 2006, Vol.22(12), pp.1571-1575 |
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| creator | TAKEHARA, Kô MORINAGA, Yuki NAKASHIMA, Shinya MATSUOKA, Shiro KAMAYA, Hiroshi UEDA, Issaku |
| description | With the fluorescence probe of 8-anilino-1-naphthalenesulfonate (ANS), the binding modes of terminally substituted alkane analogues (CnX; X = COOH, OH, CHO, NH3, CONH2) to bovine serum albumin (BSA) were investigated using a competitive binding technique. The Scatchard plot of the fluorometric titration of BSA with ANS showed that the maximum binding number of ANS, nmax, was 3.81, with the binding constant, Kbnd, of 1.42 × 106 mol-1 dm3. The binding modes of CnX to BSA were analyzed based on the fluorometric titration of the ANS and BSA mixture with CnX. CnCOOH completely displaced the ANS bound to BSA, whereas CnOH and CnCHO displaced only about 40% of the ANS bound to BSA. In contrast, CnNH2 and CnCONH2 displaced very little bound ANS. By comparing these results, we classified the binding modes of CnX to BSA into three types. Two of them are detectable with the ANS fluorescence and the remaining one is not detectable with the fluorescence. |
| doi_str_mv | 10.2116/analsci.22.1571 |
| format | Article |
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The Scatchard plot of the fluorometric titration of BSA with ANS showed that the maximum binding number of ANS, nmax, was 3.81, with the binding constant, Kbnd, of 1.42 × 106 mol-1 dm3. The binding modes of CnX to BSA were analyzed based on the fluorometric titration of the ANS and BSA mixture with CnX. CnCOOH completely displaced the ANS bound to BSA, whereas CnOH and CnCHO displaced only about 40% of the ANS bound to BSA. In contrast, CnNH2 and CnCONH2 displaced very little bound ANS. By comparing these results, we classified the binding modes of CnX to BSA into three types. Two of them are detectable with the ANS fluorescence and the remaining one is not detectable with the fluorescence.</description><identifier>ISSN: 0910-6340</identifier><identifier>EISSN: 1348-2246</identifier><identifier>DOI: 10.2116/analsci.22.1571</identifier><identifier>PMID: 17159317</identifier><language>eng</language><publisher>Japan: The Japan Society for Analytical Chemistry</publisher><subject>Alkanes - chemistry ; Animals ; Binding, Competitive ; Cattle ; Classification ; Fluorescence ; Fluorescent Dyes ; Protein Binding ; Serum Albumin, Bovine - chemistry ; Serum Albumin, Bovine - metabolism ; Titrimetry</subject><ispartof>Analytical Sciences, 2006, Vol.22(12), pp.1571-1575</ispartof><rights>2006 by The Japan Society for Analytical Chemistry</rights><rights>Copyright Japan Science and Technology Agency 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c561t-45e7ef291a83e3d1412859a900a81d3c2f270bdd547c47f16e504879f9cccee33</citedby><cites>FETCH-LOGICAL-c561t-45e7ef291a83e3d1412859a900a81d3c2f270bdd547c47f16e504879f9cccee33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1876,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17159317$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>TAKEHARA, Kô</creatorcontrib><creatorcontrib>MORINAGA, Yuki</creatorcontrib><creatorcontrib>NAKASHIMA, Shinya</creatorcontrib><creatorcontrib>MATSUOKA, Shiro</creatorcontrib><creatorcontrib>KAMAYA, Hiroshi</creatorcontrib><creatorcontrib>UEDA, Issaku</creatorcontrib><title>Classification of the Binding Modes in Bovine Serum Albumin Using Terminally Substituted Alkane Analogues</title><title>Analytical Sciences</title><addtitle>Anal Sci</addtitle><description>With the fluorescence probe of 8-anilino-1-naphthalenesulfonate (ANS), the binding modes of terminally substituted alkane analogues (CnX; X = COOH, OH, CHO, NH3, CONH2) to bovine serum albumin (BSA) were investigated using a competitive binding technique. The Scatchard plot of the fluorometric titration of BSA with ANS showed that the maximum binding number of ANS, nmax, was 3.81, with the binding constant, Kbnd, of 1.42 × 106 mol-1 dm3. The binding modes of CnX to BSA were analyzed based on the fluorometric titration of the ANS and BSA mixture with CnX. CnCOOH completely displaced the ANS bound to BSA, whereas CnOH and CnCHO displaced only about 40% of the ANS bound to BSA. In contrast, CnNH2 and CnCONH2 displaced very little bound ANS. By comparing these results, we classified the binding modes of CnX to BSA into three types. Two of them are detectable with the ANS fluorescence and the remaining one is not detectable with the fluorescence.</description><subject>Alkanes - chemistry</subject><subject>Animals</subject><subject>Binding, Competitive</subject><subject>Cattle</subject><subject>Classification</subject><subject>Fluorescence</subject><subject>Fluorescent Dyes</subject><subject>Protein Binding</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Serum Albumin, Bovine - metabolism</subject><subject>Titrimetry</subject><issn>0910-6340</issn><issn>1348-2246</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc1r3DAUxEVpaLbbnnsrgkJu3ujpw7KPm6VpCwk9JDkLrfy80da2Usku5L-PzJqU9iIh6fdGwwwhn4BtOEB5aQfbJec3nG9AaXhDViBkVXAuy7dkxWpgRSkkOyfvUzoyBrzi_B05Bw2qFqBXxO86m5JvvbOjDwMNLR0fkV75ofHDgd6GBhP1A70Kf_yA9A7j1NNtt5_6fPmQZuYeYz7Yrnumd9M-jX6cRmwy9MvmiW1-CYcJ0wdy1maz-HHZ1-Th-uv97ntx8_Pbj932pnCqhLGQCjW2vAZbCRQNyOxZ1bZmzFbQCMdbrtm-aZTUTuoWSlRMVrpua-ccohBrcnHSfYrhd_53NL1PDrsuuwlTMmXFBZdMZ_DLf-AxTHEO1ICUlVJ8DmlNLk-UiyGliK15ir638dkAM3MHZunAcG7mDvLE50V32vfY_OWX0DNwfQKOabQHfAVsHL3r8B9Bvqyz8ivgHm00OIgXMLCczw</recordid><startdate>20061201</startdate><enddate>20061201</enddate><creator>TAKEHARA, Kô</creator><creator>MORINAGA, Yuki</creator><creator>NAKASHIMA, Shinya</creator><creator>MATSUOKA, Shiro</creator><creator>KAMAYA, Hiroshi</creator><creator>UEDA, Issaku</creator><general>The Japan Society for Analytical Chemistry</general><general>Japan Science and Technology Agency</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>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SE</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>FR3</scope><scope>H8G</scope><scope>JG9</scope><scope>L7M</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20061201</creationdate><title>Classification of the Binding Modes in Bovine Serum Albumin Using Terminally Substituted Alkane Analogues</title><author>TAKEHARA, Kô ; MORINAGA, Yuki ; NAKASHIMA, Shinya ; MATSUOKA, Shiro ; KAMAYA, Hiroshi ; UEDA, Issaku</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c561t-45e7ef291a83e3d1412859a900a81d3c2f270bdd547c47f16e504879f9cccee33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Alkanes - chemistry</topic><topic>Animals</topic><topic>Binding, Competitive</topic><topic>Cattle</topic><topic>Classification</topic><topic>Fluorescence</topic><topic>Fluorescent Dyes</topic><topic>Protein Binding</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Serum Albumin, Bovine - metabolism</topic><topic>Titrimetry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>TAKEHARA, Kô</creatorcontrib><creatorcontrib>MORINAGA, Yuki</creatorcontrib><creatorcontrib>NAKASHIMA, Shinya</creatorcontrib><creatorcontrib>MATSUOKA, Shiro</creatorcontrib><creatorcontrib>KAMAYA, Hiroshi</creatorcontrib><creatorcontrib>UEDA, Issaku</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Copper Technical Reference Library</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical Sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>TAKEHARA, Kô</au><au>MORINAGA, Yuki</au><au>NAKASHIMA, Shinya</au><au>MATSUOKA, Shiro</au><au>KAMAYA, Hiroshi</au><au>UEDA, Issaku</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Classification of the Binding Modes in Bovine Serum Albumin Using Terminally Substituted Alkane Analogues</atitle><jtitle>Analytical Sciences</jtitle><addtitle>Anal Sci</addtitle><date>2006-12-01</date><risdate>2006</risdate><volume>22</volume><issue>12</issue><spage>1571</spage><epage>1575</epage><pages>1571-1575</pages><issn>0910-6340</issn><eissn>1348-2246</eissn><abstract>With the fluorescence probe of 8-anilino-1-naphthalenesulfonate (ANS), the binding modes of terminally substituted alkane analogues (CnX; X = COOH, OH, CHO, NH3, CONH2) to bovine serum albumin (BSA) were investigated using a competitive binding technique. The Scatchard plot of the fluorometric titration of BSA with ANS showed that the maximum binding number of ANS, nmax, was 3.81, with the binding constant, Kbnd, of 1.42 × 106 mol-1 dm3. The binding modes of CnX to BSA were analyzed based on the fluorometric titration of the ANS and BSA mixture with CnX. CnCOOH completely displaced the ANS bound to BSA, whereas CnOH and CnCHO displaced only about 40% of the ANS bound to BSA. In contrast, CnNH2 and CnCONH2 displaced very little bound ANS. By comparing these results, we classified the binding modes of CnX to BSA into three types. Two of them are detectable with the ANS fluorescence and the remaining one is not detectable with the fluorescence.</abstract><cop>Japan</cop><pub>The Japan Society for Analytical Chemistry</pub><pmid>17159317</pmid><doi>10.2116/analsci.22.1571</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Alkanes - chemistry Animals Binding, Competitive Cattle Classification Fluorescence Fluorescent Dyes Protein Binding Serum Albumin, Bovine - chemistry Serum Albumin, Bovine - metabolism Titrimetry |
| title | Classification of the Binding Modes in Bovine Serum Albumin Using Terminally Substituted Alkane Analogues |
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