In Situ Studies of Protein Adsorptions on Poly(pyrrole-co-pyrrole propylic acid) Film by Electrochemical Surface Plasmon Resonance
Poly(pyrrole-co-pyrrole propylic acid) (PPy/PPa) composite films were prepared for the first time by electrochemical copolymerization in mixed pyrrole propylic acid (Pa) and pyrrole solutions. The electrochemical growth process was investigated by in situ electrochemical surface plasmon resonance (E...
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| Veröffentlicht in: | Langmuir 2007-02, Vol.23 (5), p.2761-2767 |
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| creator | Hu, Weihua Li, Chang Ming Cui, Xiaoqiang Dong, Hua Zhou, Qin |
| description | Poly(pyrrole-co-pyrrole propylic acid) (PPy/PPa) composite films were prepared for the first time by electrochemical copolymerization in mixed pyrrole propylic acid (Pa) and pyrrole solutions. The electrochemical growth process was investigated by in situ electrochemical surface plasmon resonance (ESPR). Atomic force microscopy and Fourier transform infrared spectroscopy were applied to characterize the prepared films. Using bovine serum albumin as a model protein, the adsorption kinetics of the protein on PPy/PPa films were studied in situ by SPR. The composition of Pa, the isoelectric point of proteins, the pH of buffers, and surfactant treatment showed dramatic effects on the protein adsorption on the PPy/PPa film. Experimental results indicated that the electrostatic interaction between the PPy/PPa film and proteins plays a critical role in protein adsorption and provided a novel strategy to efficiently immobilize proteins and to reduce nonspecific bindings of proteins in an immunobiosensor. |
| doi_str_mv | 10.1021/la063024d |
| format | Article |
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The electrochemical growth process was investigated by in situ electrochemical surface plasmon resonance (ESPR). Atomic force microscopy and Fourier transform infrared spectroscopy were applied to characterize the prepared films. Using bovine serum albumin as a model protein, the adsorption kinetics of the protein on PPy/PPa films were studied in situ by SPR. The composition of Pa, the isoelectric point of proteins, the pH of buffers, and surfactant treatment showed dramatic effects on the protein adsorption on the PPy/PPa film. Experimental results indicated that the electrostatic interaction between the PPy/PPa film and proteins plays a critical role in protein adsorption and provided a novel strategy to efficiently immobilize proteins and to reduce nonspecific bindings of proteins in an immunobiosensor.</description><identifier>ISSN: 0743-7463</identifier><identifier>EISSN: 1520-5827</identifier><identifier>DOI: 10.1021/la063024d</identifier><identifier>PMID: 17309219</identifier><identifier>CODEN: LANGD5</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Adsorption ; Animals ; Biosensing Techniques - instrumentation ; Buffers ; Cattle ; Chemistry ; Colloidal state and disperse state ; Electrochemistry ; Electrochemistry - methods ; Exact sciences and technology ; General and physical chemistry ; Hydrogen-Ion Concentration ; Microscopy, Atomic Force - methods ; Propionates - chemistry ; Proteins - chemistry ; Pyrroles - chemistry ; Serum Albumin, Bovine - chemistry ; Spectroscopy, Fourier Transform Infrared ; Surface physical chemistry ; Surface Plasmon Resonance - methods ; Surface Properties ; Surface-Active Agents - chemistry</subject><ispartof>Langmuir, 2007-02, Vol.23 (5), p.2761-2767</ispartof><rights>Copyright © 2007 American Chemical Society</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a381t-bf5b19f138b920189608895feb2b08287ef3b663dc82d41dbf5a24466e1ee3173</citedby><cites>FETCH-LOGICAL-a381t-bf5b19f138b920189608895feb2b08287ef3b663dc82d41dbf5a24466e1ee3173</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/la063024d$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/la063024d$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2764,27075,27923,27924,56737,56787</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18841543$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17309219$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hu, Weihua</creatorcontrib><creatorcontrib>Li, Chang Ming</creatorcontrib><creatorcontrib>Cui, Xiaoqiang</creatorcontrib><creatorcontrib>Dong, Hua</creatorcontrib><creatorcontrib>Zhou, Qin</creatorcontrib><title>In Situ Studies of Protein Adsorptions on Poly(pyrrole-co-pyrrole propylic acid) Film by Electrochemical Surface Plasmon Resonance</title><title>Langmuir</title><addtitle>Langmuir</addtitle><description>Poly(pyrrole-co-pyrrole propylic acid) (PPy/PPa) composite films were prepared for the first time by electrochemical copolymerization in mixed pyrrole propylic acid (Pa) and pyrrole solutions. The electrochemical growth process was investigated by in situ electrochemical surface plasmon resonance (ESPR). Atomic force microscopy and Fourier transform infrared spectroscopy were applied to characterize the prepared films. Using bovine serum albumin as a model protein, the adsorption kinetics of the protein on PPy/PPa films were studied in situ by SPR. The composition of Pa, the isoelectric point of proteins, the pH of buffers, and surfactant treatment showed dramatic effects on the protein adsorption on the PPy/PPa film. Experimental results indicated that the electrostatic interaction between the PPy/PPa film and proteins plays a critical role in protein adsorption and provided a novel strategy to efficiently immobilize proteins and to reduce nonspecific bindings of proteins in an immunobiosensor.</description><subject>Adsorption</subject><subject>Animals</subject><subject>Biosensing Techniques - instrumentation</subject><subject>Buffers</subject><subject>Cattle</subject><subject>Chemistry</subject><subject>Colloidal state and disperse state</subject><subject>Electrochemistry</subject><subject>Electrochemistry - methods</subject><subject>Exact sciences and technology</subject><subject>General and physical chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Microscopy, Atomic Force - methods</subject><subject>Propionates - chemistry</subject><subject>Proteins - chemistry</subject><subject>Pyrroles - chemistry</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Surface physical chemistry</subject><subject>Surface Plasmon Resonance - methods</subject><subject>Surface Properties</subject><subject>Surface-Active Agents - chemistry</subject><issn>0743-7463</issn><issn>1520-5827</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkMtu1DAUQC0EosPAgh9A3oDoIuBXEntZlRYqDWJgimBnOc6NcHHiYCcS2fLlGE3U2bCyZR8d3XsQek7JG0oYfesNqThhon2ANrRkpCglqx-iDakFL2pR8TP0JKU7QojiQj1GZ7TmRDGqNujPzYAPbprxYZpbBwmHDu9jmMAN-KJNIY6TC0N-HvA--OX1uMQYPBQ2FOsVjzGMi3cWG-vac3ztfI-bBV95sFMM9gf0zhqPD3PsjAW89yb1WfcFUhjMYOEpetQZn-DZem7R1-ur28sPxe7T-5vLi11huKRT0XRlQ1VHuWwUI1Sqikipyg4a1hDJZA0db6qKt1ayVtA284YJUVVAAXjeeIteHb154F8zpEn3Llnw3gwQ5qQrRRin2bBF50fQxpBShE6P0fUmLpoS_S-4vg-e2RerdG56aE_kWjgDL1fApJyhi3lll06clIKWgmeuOHIuTfD7_t_En7qqeV3q2_1Bfxbf38mPO6q_nbzGJn0X5jjkdv8Z8C-HJqRB</recordid><startdate>20070227</startdate><enddate>20070227</enddate><creator>Hu, Weihua</creator><creator>Li, Chang Ming</creator><creator>Cui, Xiaoqiang</creator><creator>Dong, Hua</creator><creator>Zhou, Qin</creator><general>American Chemical Society</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>20070227</creationdate><title>In Situ Studies of Protein Adsorptions on Poly(pyrrole-co-pyrrole propylic acid) Film by Electrochemical Surface Plasmon Resonance</title><author>Hu, Weihua ; Li, Chang Ming ; Cui, Xiaoqiang ; Dong, Hua ; Zhou, Qin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a381t-bf5b19f138b920189608895feb2b08287ef3b663dc82d41dbf5a24466e1ee3173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adsorption</topic><topic>Animals</topic><topic>Biosensing Techniques - instrumentation</topic><topic>Buffers</topic><topic>Cattle</topic><topic>Chemistry</topic><topic>Colloidal state and disperse state</topic><topic>Electrochemistry</topic><topic>Electrochemistry - methods</topic><topic>Exact sciences and technology</topic><topic>General and physical chemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Microscopy, Atomic Force - methods</topic><topic>Propionates - chemistry</topic><topic>Proteins - chemistry</topic><topic>Pyrroles - chemistry</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>Surface physical chemistry</topic><topic>Surface Plasmon Resonance - methods</topic><topic>Surface Properties</topic><topic>Surface-Active Agents - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hu, Weihua</creatorcontrib><creatorcontrib>Li, Chang Ming</creatorcontrib><creatorcontrib>Cui, Xiaoqiang</creatorcontrib><creatorcontrib>Dong, Hua</creatorcontrib><creatorcontrib>Zhou, Qin</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>Langmuir</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hu, Weihua</au><au>Li, Chang Ming</au><au>Cui, Xiaoqiang</au><au>Dong, Hua</au><au>Zhou, Qin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In Situ Studies of Protein Adsorptions on Poly(pyrrole-co-pyrrole propylic acid) Film by Electrochemical Surface Plasmon Resonance</atitle><jtitle>Langmuir</jtitle><addtitle>Langmuir</addtitle><date>2007-02-27</date><risdate>2007</risdate><volume>23</volume><issue>5</issue><spage>2761</spage><epage>2767</epage><pages>2761-2767</pages><issn>0743-7463</issn><eissn>1520-5827</eissn><coden>LANGD5</coden><abstract>Poly(pyrrole-co-pyrrole propylic acid) (PPy/PPa) composite films were prepared for the first time by electrochemical copolymerization in mixed pyrrole propylic acid (Pa) and pyrrole solutions. The electrochemical growth process was investigated by in situ electrochemical surface plasmon resonance (ESPR). Atomic force microscopy and Fourier transform infrared spectroscopy were applied to characterize the prepared films. Using bovine serum albumin as a model protein, the adsorption kinetics of the protein on PPy/PPa films were studied in situ by SPR. The composition of Pa, the isoelectric point of proteins, the pH of buffers, and surfactant treatment showed dramatic effects on the protein adsorption on the PPy/PPa film. Experimental results indicated that the electrostatic interaction between the PPy/PPa film and proteins plays a critical role in protein adsorption and provided a novel strategy to efficiently immobilize proteins and to reduce nonspecific bindings of proteins in an immunobiosensor.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>17309219</pmid><doi>10.1021/la063024d</doi><tpages>7</tpages></addata></record> |
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| subjects | Adsorption Animals Biosensing Techniques - instrumentation Buffers Cattle Chemistry Colloidal state and disperse state Electrochemistry Electrochemistry - methods Exact sciences and technology General and physical chemistry Hydrogen-Ion Concentration Microscopy, Atomic Force - methods Propionates - chemistry Proteins - chemistry Pyrroles - chemistry Serum Albumin, Bovine - chemistry Spectroscopy, Fourier Transform Infrared Surface physical chemistry Surface Plasmon Resonance - methods Surface Properties Surface-Active Agents - chemistry |
| title | In Situ Studies of Protein Adsorptions on Poly(pyrrole-co-pyrrole propylic acid) Film by Electrochemical Surface Plasmon Resonance |
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