Binding of cationic porphyrin to human serum albumin studied using comprehensive spectroscopic methods
The interaction between cationic porphyrin, a potential valuable anti-tumor and antibiotic drug, and human serum albumin (HSA) was investigated using spectroscopy methods. The binding constants were obtained using fluorescence quenching method (KSV = (3.24 ± 0.29) × 104 M−1) and surface plasmon reso...
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| Veröffentlicht in: | Journal of pharmaceutical sciences 2009-01, Vol.98 (1), p.105-113 |
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| creator | Zhou, Bo Zhang, Zhi Zhang, Yue Li, Ran Xiao, Qi Liu, Yi Li, ZaoYing |
| description | The interaction between cationic porphyrin, a potential valuable anti-tumor and antibiotic drug, and human serum albumin (HSA) was investigated using spectroscopy methods. The binding constants were obtained using fluorescence quenching method (KSV = (3.24 ± 0.29) × 104 M−1) and surface plasmon resonance (SPR) spectroscopy (KA = (6.287 ± 0.407) × 104 M−1). The association rate constant (ka = 1622 ± 72.9 M−1 s−1) and dissociation rate constant (Kd = 0.02589 ± 0.0024 s−1) of the binding process were also calculated. Compared with the two results, it was known that one of the binding sites was near the tryptophan residue and also there existed other binding sites. The Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) spectroscopy indicated that the confirmation of HSA was nearly not affected with the addition of porphyrin. © 2008 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 98:105–113, 2009 |
| doi_str_mv | 10.1002/jps.21413 |
| format | Article |
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The binding constants were obtained using fluorescence quenching method (KSV = (3.24 ± 0.29) × 104 M−1) and surface plasmon resonance (SPR) spectroscopy (KA = (6.287 ± 0.407) × 104 M−1). The association rate constant (ka = 1622 ± 72.9 M−1 s−1) and dissociation rate constant (Kd = 0.02589 ± 0.0024 s−1) of the binding process were also calculated. Compared with the two results, it was known that one of the binding sites was near the tryptophan residue and also there existed other binding sites. The Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) spectroscopy indicated that the confirmation of HSA was nearly not affected with the addition of porphyrin. © 2008 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 98:105–113, 2009</description><identifier>ISSN: 0022-3549</identifier><identifier>EISSN: 1520-6017</identifier><identifier>DOI: 10.1002/jps.21413</identifier><identifier>PMID: 18464274</identifier><identifier>CODEN: JPMSAE</identifier><language>eng</language><publisher>Hoboken: Elsevier Inc</publisher><subject>binding ; Biological and medical sciences ; Cations - analysis ; Cations - metabolism ; Circular Dichroism ; fluorescence quenching ; General pharmacology ; HSA ; Humans ; Medical sciences ; Pharmaceutical technology. Pharmaceutical industry ; Pharmacology. Drug treatments ; porphyrin ; Porphyrins - metabolism ; Porphyrins - physiology ; Protein Binding - physiology ; Protein Conformation ; Protein Structure, Secondary ; Serum Albumin - analysis ; Serum Albumin - metabolism ; Spectrometry, Fluorescence ; Spectroscopy, Fourier Transform Infrared ; SPR ; Surface Plasmon Resonance</subject><ispartof>Journal of pharmaceutical sciences, 2009-01, Vol.98 (1), p.105-113</ispartof><rights>2008 Wiley-Liss, Inc.</rights><rights>Copyright © 2008 Wiley‐Liss, Inc.</rights><rights>2009 INIST-CNRS</rights><rights>(c) 2008 Wiley-Liss, Inc. and the American Pharmacists Association</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4353-4f2669e00fa619b1fdaf96cfdd2eba4282765546c69c2f345b7e7d2c223b28683</citedby><cites>FETCH-LOGICAL-c4353-4f2669e00fa619b1fdaf96cfdd2eba4282765546c69c2f345b7e7d2c223b28683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjps.21413$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjps.21413$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,4023,27922,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21006206$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18464274$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhou, Bo</creatorcontrib><creatorcontrib>Zhang, Zhi</creatorcontrib><creatorcontrib>Zhang, Yue</creatorcontrib><creatorcontrib>Li, Ran</creatorcontrib><creatorcontrib>Xiao, Qi</creatorcontrib><creatorcontrib>Liu, Yi</creatorcontrib><creatorcontrib>Li, ZaoYing</creatorcontrib><title>Binding of cationic porphyrin to human serum albumin studied using comprehensive spectroscopic methods</title><title>Journal of pharmaceutical sciences</title><addtitle>J. Pharm. Sci</addtitle><description>The interaction between cationic porphyrin, a potential valuable anti-tumor and antibiotic drug, and human serum albumin (HSA) was investigated using spectroscopy methods. The binding constants were obtained using fluorescence quenching method (KSV = (3.24 ± 0.29) × 104 M−1) and surface plasmon resonance (SPR) spectroscopy (KA = (6.287 ± 0.407) × 104 M−1). The association rate constant (ka = 1622 ± 72.9 M−1 s−1) and dissociation rate constant (Kd = 0.02589 ± 0.0024 s−1) of the binding process were also calculated. Compared with the two results, it was known that one of the binding sites was near the tryptophan residue and also there existed other binding sites. The Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) spectroscopy indicated that the confirmation of HSA was nearly not affected with the addition of porphyrin. © 2008 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 98:105–113, 2009</description><subject>binding</subject><subject>Biological and medical sciences</subject><subject>Cations - analysis</subject><subject>Cations - metabolism</subject><subject>Circular Dichroism</subject><subject>fluorescence quenching</subject><subject>General pharmacology</subject><subject>HSA</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Pharmaceutical technology. Pharmaceutical industry</subject><subject>Pharmacology. Drug treatments</subject><subject>porphyrin</subject><subject>Porphyrins - metabolism</subject><subject>Porphyrins - physiology</subject><subject>Protein Binding - physiology</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Serum Albumin - analysis</subject><subject>Serum Albumin - metabolism</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>SPR</subject><subject>Surface Plasmon Resonance</subject><issn>0022-3549</issn><issn>1520-6017</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kc1u1DAURi0EokNhwQugbEBikdZ_cZIlU9FCNSpIgFhajn3NuCRx6psU5u1xmaFsYGXJPt937WNCnjN6wijlp9cTnnAmmXhAVqzitFSU1Q_JKp_xUlSyPSJPEK8ppYpW1WNyxBqpJK_livh1GF0YvxXRF9bMIY7BFlNM03aXwljMsdgugxkLhLQMhem7ZcjbOC8ugCsWvIvaOEwJtjBiuIUCJ7BzimjjlKsGmLfR4VPyyJse4dlhPSZfzt9-PntXbj5cvD97symtFJUopedKtUCpN4q1HfPO-FZZ7xyHzkje8FpVlVRWtZZ7Iauuhtpxy7noeKMacUxe7XunFG8WwFkPAS30vRkhLqiVqnnTUJbB13vQ5qtiAq-nFAaTdppRfSdVZ6n6t9TMvjiULt0A7i95sJiBlwfAoDW9T2a0Ae85nvsUpypzp3vuR-hh9_-J-vLjpz-jy30i4Aw_7xMmfdeqFnWlv15d6M1aXLbnVxu9zrzY85Al3wZIGm2A0YILKX-LdjH844G_ADGpsFA</recordid><startdate>200901</startdate><enddate>200901</enddate><creator>Zhou, Bo</creator><creator>Zhang, Zhi</creator><creator>Zhang, Yue</creator><creator>Li, Ran</creator><creator>Xiao, Qi</creator><creator>Liu, Yi</creator><creator>Li, ZaoYing</creator><general>Elsevier Inc</general><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley</general><general>American Pharmaceutical Association</general><scope>BSCLL</scope><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>7X8</scope></search><sort><creationdate>200901</creationdate><title>Binding of cationic porphyrin to human serum albumin studied using comprehensive spectroscopic methods</title><author>Zhou, Bo ; Zhang, Zhi ; Zhang, Yue ; Li, Ran ; Xiao, Qi ; Liu, Yi ; Li, ZaoYing</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4353-4f2669e00fa619b1fdaf96cfdd2eba4282765546c69c2f345b7e7d2c223b28683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>binding</topic><topic>Biological and medical sciences</topic><topic>Cations - analysis</topic><topic>Cations - metabolism</topic><topic>Circular Dichroism</topic><topic>fluorescence quenching</topic><topic>General pharmacology</topic><topic>HSA</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Pharmaceutical technology. Pharmaceutical industry</topic><topic>Pharmacology. Drug treatments</topic><topic>porphyrin</topic><topic>Porphyrins - metabolism</topic><topic>Porphyrins - physiology</topic><topic>Protein Binding - physiology</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Serum Albumin - analysis</topic><topic>Serum Albumin - metabolism</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>SPR</topic><topic>Surface Plasmon Resonance</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhou, Bo</creatorcontrib><creatorcontrib>Zhang, Zhi</creatorcontrib><creatorcontrib>Zhang, Yue</creatorcontrib><creatorcontrib>Li, Ran</creatorcontrib><creatorcontrib>Xiao, Qi</creatorcontrib><creatorcontrib>Liu, Yi</creatorcontrib><creatorcontrib>Li, ZaoYing</creatorcontrib><collection>Istex</collection><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>MEDLINE - Academic</collection><jtitle>Journal of pharmaceutical sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhou, Bo</au><au>Zhang, Zhi</au><au>Zhang, Yue</au><au>Li, Ran</au><au>Xiao, Qi</au><au>Liu, Yi</au><au>Li, ZaoYing</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding of cationic porphyrin to human serum albumin studied using comprehensive spectroscopic methods</atitle><jtitle>Journal of pharmaceutical sciences</jtitle><addtitle>J. Pharm. Sci</addtitle><date>2009-01</date><risdate>2009</risdate><volume>98</volume><issue>1</issue><spage>105</spage><epage>113</epage><pages>105-113</pages><issn>0022-3549</issn><eissn>1520-6017</eissn><coden>JPMSAE</coden><abstract>The interaction between cationic porphyrin, a potential valuable anti-tumor and antibiotic drug, and human serum albumin (HSA) was investigated using spectroscopy methods. The binding constants were obtained using fluorescence quenching method (KSV = (3.24 ± 0.29) × 104 M−1) and surface plasmon resonance (SPR) spectroscopy (KA = (6.287 ± 0.407) × 104 M−1). The association rate constant (ka = 1622 ± 72.9 M−1 s−1) and dissociation rate constant (Kd = 0.02589 ± 0.0024 s−1) of the binding process were also calculated. Compared with the two results, it was known that one of the binding sites was near the tryptophan residue and also there existed other binding sites. The Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) spectroscopy indicated that the confirmation of HSA was nearly not affected with the addition of porphyrin. © 2008 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 98:105–113, 2009</abstract><cop>Hoboken</cop><pub>Elsevier Inc</pub><pmid>18464274</pmid><doi>10.1002/jps.21413</doi><tpages>9</tpages></addata></record> |
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| subjects | binding Biological and medical sciences Cations - analysis Cations - metabolism Circular Dichroism fluorescence quenching General pharmacology HSA Humans Medical sciences Pharmaceutical technology. Pharmaceutical industry Pharmacology. Drug treatments porphyrin Porphyrins - metabolism Porphyrins - physiology Protein Binding - physiology Protein Conformation Protein Structure, Secondary Serum Albumin - analysis Serum Albumin - metabolism Spectrometry, Fluorescence Spectroscopy, Fourier Transform Infrared SPR Surface Plasmon Resonance |
| title | Binding of cationic porphyrin to human serum albumin studied using comprehensive spectroscopic methods |
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