Voltammetric and Spectroscopic Evaluation of the Interactions of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol with Bovine and Human Serum Albumins at Physiological pH
The bindings of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol (PMNO) to bovine and human serum albumins (abbreviated as BSA and HSA, respectively) in 0.05 M phosphate buffer (abbreviated as PB) solution of pH 7.40 were analysed via square-wave voltammetry (SWV) and UV-Vis absorption spectrosco...
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Veröffentlicht in: | Russian journal of electrochemistry 2022-09, Vol.58 (9), p.835-843 |
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creator | Ender Biçer Tanju, Neslihan Özdemir Macit, Mustafa |
description | The bindings of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol (PMNO) to bovine and human serum albumins (abbreviated as BSA and HSA, respectively) in 0.05 M phosphate buffer (abbreviated as PB) solution of pH 7.40 were analysed via square-wave voltammetry (SWV) and UV-Vis absorption spectroscopy. By using decreases in the reduction current of PMNO with addition of the serum albumins, the binding constants of the interactions between PMNO and BSA and HSA for a binding ratio of 1 : 1 were found to be 1.97 × 10
8
and 1.78 × 10
6
M
−1
, respectively. From the UV-Vis absorption spectroscopy data at 443 nm, the binding constant values for PMNO–BSA and PMNO–HSA systems were obtained to be 1.37 × 10
7
and 1.39 × 10
6
M
−1
, respectively. |
doi_str_mv | 10.1134/S1023193522090038 |
format | Article |
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8
and 1.78 × 10
6
M
−1
, respectively. From the UV-Vis absorption spectroscopy data at 443 nm, the binding constant values for PMNO–BSA and PMNO–HSA systems were obtained to be 1.37 × 10
7
and 1.39 × 10
6
M
−1
, respectively.</description><identifier>ISSN: 1023-1935</identifier><identifier>EISSN: 1608-3342</identifier><identifier>DOI: 10.1134/S1023193522090038</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Absorption spectroscopy ; Binding ; Cattle ; Chemistry ; Chemistry and Materials Science ; Electrochemistry ; Physical Chemistry ; Serum albumin ; Voltammetry</subject><ispartof>Russian journal of electrochemistry, 2022-09, Vol.58 (9), p.835-843</ispartof><rights>Pleiades Publishing, Ltd. 2022. ISSN 1023-1935, Russian Journal of Electrochemistry, 2022, Vol. 58, No. 9, pp. 835–843. © Pleiades Publishing, Ltd., 2022.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c198t-b0d6d487187fe65677f9a1bdbf52a39212eca2b4150067d99743bfec981897d43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S1023193522090038$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S1023193522090038$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Ender Biçer</creatorcontrib><creatorcontrib>Tanju, Neslihan Özdemir</creatorcontrib><creatorcontrib>Macit, Mustafa</creatorcontrib><title>Voltammetric and Spectroscopic Evaluation of the Interactions of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol with Bovine and Human Serum Albumins at Physiological pH</title><title>Russian journal of electrochemistry</title><addtitle>Russ J Electrochem</addtitle><description>The bindings of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol (PMNO) to bovine and human serum albumins (abbreviated as BSA and HSA, respectively) in 0.05 M phosphate buffer (abbreviated as PB) solution of pH 7.40 were analysed via square-wave voltammetry (SWV) and UV-Vis absorption spectroscopy. By using decreases in the reduction current of PMNO with addition of the serum albumins, the binding constants of the interactions between PMNO and BSA and HSA for a binding ratio of 1 : 1 were found to be 1.97 × 10
8
and 1.78 × 10
6
M
−1
, respectively. From the UV-Vis absorption spectroscopy data at 443 nm, the binding constant values for PMNO–BSA and PMNO–HSA systems were obtained to be 1.37 × 10
7
and 1.39 × 10
6
M
−1
, respectively.</description><subject>Absorption spectroscopy</subject><subject>Binding</subject><subject>Cattle</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Electrochemistry</subject><subject>Physical Chemistry</subject><subject>Serum albumin</subject><subject>Voltammetry</subject><issn>1023-1935</issn><issn>1608-3342</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNp1Uc1u1DAQjhBIlMIDcLPEZfdg8NhJHB9LtbCVKoG0wDVyHKdx5djBdlryULwjDovEAXGa0Tffj2amKF4DeQvAyncnIJSBYBWlRBDCmifFBdSkwYyV9Gnu8xhv8-fFixjvCSENB3FR_PzmbZLTpFMwCknXo9OsVQo-Kj9n5PAg7SKT8Q75AaVRoxuXdJBqg-KG7Q57DHi3K_E8aud_rFtZrZmM8_vsO6527-Q8plFa7TDF3qJHk0b03j8Yp39nHpdJOnTSYZnQle2WrI1IJvR5XKPx1t8ZJS2ajy-LZ4O0Ub_6Uy-Lrx8OX66P-PbTx5vrq1usQDQJd6Sv-zIv2PBB11XN-SAkdH03VFQyQYFqJWlXQkVIzXsheMm6QSvRQCN4X7LL4s3Zdw7--6Jjau_9ElyObCmHuqqAE5ZZcGapfK4Y9NDOwUwyrC2QdvtK-89XsoaeNTFz3Z0Of53_L_oFF8SQFw</recordid><startdate>20220901</startdate><enddate>20220901</enddate><creator>Ender Biçer</creator><creator>Tanju, Neslihan Özdemir</creator><creator>Macit, Mustafa</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20220901</creationdate><title>Voltammetric and Spectroscopic Evaluation of the Interactions of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol with Bovine and Human Serum Albumins at Physiological pH</title><author>Ender Biçer ; Tanju, Neslihan Özdemir ; Macit, Mustafa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c198t-b0d6d487187fe65677f9a1bdbf52a39212eca2b4150067d99743bfec981897d43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Absorption spectroscopy</topic><topic>Binding</topic><topic>Cattle</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Electrochemistry</topic><topic>Physical Chemistry</topic><topic>Serum albumin</topic><topic>Voltammetry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ender Biçer</creatorcontrib><creatorcontrib>Tanju, Neslihan Özdemir</creatorcontrib><creatorcontrib>Macit, Mustafa</creatorcontrib><collection>CrossRef</collection><jtitle>Russian journal of electrochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ender Biçer</au><au>Tanju, Neslihan Özdemir</au><au>Macit, Mustafa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Voltammetric and Spectroscopic Evaluation of the Interactions of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol with Bovine and Human Serum Albumins at Physiological pH</atitle><jtitle>Russian journal of electrochemistry</jtitle><stitle>Russ J Electrochem</stitle><date>2022-09-01</date><risdate>2022</risdate><volume>58</volume><issue>9</issue><spage>835</spage><epage>843</epage><pages>835-843</pages><issn>1023-1935</issn><eissn>1608-3342</eissn><abstract>The bindings of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol (PMNO) to bovine and human serum albumins (abbreviated as BSA and HSA, respectively) in 0.05 M phosphate buffer (abbreviated as PB) solution of pH 7.40 were analysed via square-wave voltammetry (SWV) and UV-Vis absorption spectroscopy. By using decreases in the reduction current of PMNO with addition of the serum albumins, the binding constants of the interactions between PMNO and BSA and HSA for a binding ratio of 1 : 1 were found to be 1.97 × 10
8
and 1.78 × 10
6
M
−1
, respectively. From the UV-Vis absorption spectroscopy data at 443 nm, the binding constant values for PMNO–BSA and PMNO–HSA systems were obtained to be 1.37 × 10
7
and 1.39 × 10
6
M
−1
, respectively.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><doi>10.1134/S1023193522090038</doi><tpages>9</tpages></addata></record> |
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language | eng |
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subjects | Absorption spectroscopy Binding Cattle Chemistry Chemistry and Materials Science Electrochemistry Physical Chemistry Serum albumin Voltammetry |
title | Voltammetric and Spectroscopic Evaluation of the Interactions of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol with Bovine and Human Serum Albumins at Physiological pH |
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