A polypyrrole protein microarray for antibody–antigen interaction studies using a label-free detection process
Protein microarray is a promising technology that should combine rapidity and easy use with high throughput and versatility. This article describes a method in which an electrocopolymerization process is employed to graft biological molecules on to a chip so that surface plasmon resonance imaging ma...
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Veröffentlicht in: | Analytical biochemistry 2005-12, Vol.347 (2), p.193-200 |
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creator | Grosjean, Ludivine Cherif, Boutheina Mercey, Emilie Roget, André Levy, Yves Marche, Patrice Noel Villiers, Marie-Bernadette Livache, Thierry |
description | Protein microarray is a promising technology that should combine rapidity and easy use with high throughput and versatility. This article describes a method in which an electrocopolymerization process is employed to graft biological molecules on to a chip so that surface plasmon resonance imaging may be used to detect molecular interactions. Copolymerization of pyrrole-modified protein and pyrrole is an efficient grafting process which immobilizes molecules at defined positions on a gold surface. Surface plasmon resonance imaging is an optical technique that allows real-time simultaneous detection of molecular interactions on a large number of spots without labeling. This method was successfully used to analyze antibody–antigen interactions. This illustrates its high specificity and good sensitivity and demonstrates its suitability for biological studies. |
doi_str_mv | 10.1016/j.ab.2005.09.033 |
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This article describes a method in which an electrocopolymerization process is employed to graft biological molecules on to a chip so that surface plasmon resonance imaging may be used to detect molecular interactions. Copolymerization of pyrrole-modified protein and pyrrole is an efficient grafting process which immobilizes molecules at defined positions on a gold surface. Surface plasmon resonance imaging is an optical technique that allows real-time simultaneous detection of molecular interactions on a large number of spots without labeling. This method was successfully used to analyze antibody–antigen interactions. This illustrates its high specificity and good sensitivity and demonstrates its suitability for biological studies.</description><subject>Animals</subject><subject>Antibody</subject><subject>Antigen</subject><subject>Antigen-Antibody Reactions</subject><subject>Biotechnology</subject><subject>Chemistry Techniques, Analytical</subject><subject>Chemistry, Analytical</subject><subject>Chorionic Gonadotropin</subject><subject>Chorionic Gonadotropin - immunology</subject><subject>Computer Science</subject><subject>Humans</subject><subject>Immunology</subject><subject>In Vitro Techniques</subject><subject>Life Sciences</subject><subject>Muramidase</subject><subject>Muramidase - immunology</subject><subject>Polymers</subject><subject>Polypyrrole</subject><subject>Protein Array Analysis</subject><subject>Protein Array Analysis - instrumentation</subject><subject>Protein Array Analysis - methods</subject><subject>Protein microarray</subject><subject>Pyrroles</subject><subject>Surface Plasmon Resonance</subject><subject>Surface plasmon resonance imaging</subject><subject>Surface Properties</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkb2O1DAUhS0EYoeFngq5oiLhOk6cmG60AhZpJBqorRv7ZvEoP4OdrJSOd-ANeRI8ymipVlTnFt85ujqHsdcCcgFCvT_m2OYFQJWDzkHKJ2wnQKsMJOinbAcAMiuUrq_YixiPAEKUlXrOroQqlFKN2LHTnp-mfj2tIUw98VOYZvIjH7wNE4aAK--mwHGcfTu59c-v3-fzjkbux5kC2tlPI4_z4jxFvkQ_3nHkPbbUZ10g4o5m2qAUbSnGl-xZh32kVxe9Zt8_ffx2c5sdvn7-crM_ZLZsijkTlexETRUpW1RKIKLuUJOVUpeVQ5cEXY01kGqd0k3REDaOnO1qDQVKec3ebbk_sDen4AcMq5nQm9v9wfgxUhhMKqQsZSXvRcLfbnh68-dCcTaDj5b6HkealmhU00gpyv-DBchCat0kEDYwNRljoO7hCwHmvJ45GmzNeT0D2qT1kuXNJXtpB3L_DJe5EvBhAyg1d-8pmGg9jZacD6lm4yb_ePpfaTOsvA</recordid><startdate>20051215</startdate><enddate>20051215</enddate><creator>Grosjean, Ludivine</creator><creator>Cherif, Boutheina</creator><creator>Mercey, Emilie</creator><creator>Roget, André</creator><creator>Levy, Yves</creator><creator>Marche, Patrice Noel</creator><creator>Villiers, Marie-Bernadette</creator><creator>Livache, Thierry</creator><general>Elsevier Inc</general><general>Elsevier Masson</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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><orcidid>https://orcid.org/0000-0001-7976-3059</orcidid><orcidid>https://orcid.org/0000-0002-4224-3137</orcidid><orcidid>https://orcid.org/0000-0002-5549-6256</orcidid></search><sort><creationdate>20051215</creationdate><title>A polypyrrole protein microarray for antibody–antigen interaction studies using a label-free detection process</title><author>Grosjean, Ludivine ; 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subjects | Animals Antibody Antigen Antigen-Antibody Reactions Biotechnology Chemistry Techniques, Analytical Chemistry, Analytical Chorionic Gonadotropin Chorionic Gonadotropin - immunology Computer Science Humans Immunology In Vitro Techniques Life Sciences Muramidase Muramidase - immunology Polymers Polypyrrole Protein Array Analysis Protein Array Analysis - instrumentation Protein Array Analysis - methods Protein microarray Pyrroles Surface Plasmon Resonance Surface plasmon resonance imaging Surface Properties |
title | A polypyrrole protein microarray for antibody–antigen interaction studies using a label-free detection process |
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