Nanosphere Lithography as a Versatile Method to Generate Surface‐Imprinted Polymer Films for Selective Protein Recognition
Identifieur interne : 002125 ( Main/Exploration ); précédent : 002124; suivant : 002126Nanosphere Lithography as a Versatile Method to Generate Surface‐Imprinted Polymer Films for Selective Protein Recognition
Auteurs : Júlia Bognár [Hongrie] ; Júlia Sz Cs [Hongrie] ; Zsanett Dork [Hongrie] ; Viola Horváth [Hongrie] ; R Bert E. Gyurcsányi [Hongrie]Source :
- Advanced Functional Materials [ 1616-301X ] ; 2013-10-04.
English descriptors
- Teeft :
- Adsorption, Anal, Aqueous solution, Avidin, Bead, Bead conjugates, Beads, Binding isotherms, Binding sites, Bovine serum albumin, Carrier buffer, Carrier solution, Chem, Cleavable crosslinker, Compact layer, Electrical charge, Electropolymerization, Full paper, Funct, Gmbh, Heterobifunctional crosslinker, Imprinting, Imprinting factor, Kgaa, Lithography, Macromolecular template, Mater, Mips, Nanogravimetric measurements, Nanosphere, Nanosphere lithography, Polymer, Polymer surface, Polystyrene beads, Preferential growth, Protein imprinting, Protein target, Quartz, Quartz crystal resonator, Quartz crystals, Selective protein recognition, Sigma aldrich, Successive steps, Target molecule, Verlag, Verlag gmbh, Weinheim.
Abstract
A versatile approach based on nanosphere lithography is proposed to generate surface‐imprinted polymers for selective protein recognition. A layer of 750 nm diameter latex bead‐protein conjugate is deposited onto the surface of gold‐coated quartz crystals followed by the electrosynthesis of a poly(3,4‐ethylenedioxythiophene)/poly(styrenesulfonate) (PEDOT/PSS) film with thicknesses on the order of the bead radius. The removal of the polymer bead‐protein conjugates, facilitated by using a cleavable protein‐nanosphere linkage is shown to result in 2D arrays of periodic complementary size cavities. Here it is demonstrated by nanogravimetric measurements that the imprinting proceeds further at molecular level and the protein (avidin) coating of the beads generates selective recognition sites for avidin on the surface of the PEDOT/PSS film. The binding capacity of such surface‐imprinted polymer films is ca. 6.5 times higher than that of films imprinted with unmodified beads. They also exhibit excellent selectivity against analogues of avidin, i.e., extravidin, streptavidin, and neutravidin, the latter being in fact undetectable. This methodology, if coupled with properly oriented conjugation of the macromolecular template to the nanoparticles, offers the possibility of site‐directed imprinting.
A versatile approach based on nanosphere lithography is proposed to generate surface‐imprinted polymers for selective protein recognition. Nanogravimetric measurements demonstrate that the protein (avidin) coating of the nanospheres generates selective recognition sites for avidin on the surface of the PEDOT/PSS film. This methodology coupled with oriented conjugation of the macromolecular template to the nanospheres offers the possibility of site‐directed imprinting.
Url:
DOI: 10.1002/adfm.201300113
Affiliations:
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Gellért tér 4, Budapest, H‐1111</wicri:regionArea><wicri:noRegion>H‐1111</wicri:noRegion></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Hongrie</country><wicri:regionArea>Research Group for Technical Analytical Chemistry, Hungarian Academy of Sciences, Szt. Gellért tér 4, Budapest, H‐1111</wicri:regionArea><wicri:noRegion>H‐1111</wicri:noRegion></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Hongrie</country></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Hongrie</country><wicri:regionArea>Correspondence address: Department of Inorganic and Analytical Chemistry, Budapest University of Technology and Economics, Szt. Gellért tér 4, Budapest, H‐1111</wicri:regionArea><wicri:noRegion>H‐1111</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Advanced Functional Materials</title><title level="j" type="alt">ADVANCED FUNCTIONAL MATERIALS</title><idno type="ISSN">1616-301X</idno><idno type="eISSN">1616-3028</idno><imprint><biblScope unit="vol">23</biblScope><biblScope unit="issue">37</biblScope><biblScope unit="page" from="4703">4703</biblScope><biblScope unit="page" to="4709">4709</biblScope><biblScope unit="page-count">7</biblScope><publisher>WILEY‐VCH Verlag</publisher><pubPlace>Weinheim</pubPlace><date type="published" when="2013-10-04">2013-10-04</date></imprint><idno type="ISSN">1616-301X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1616-301X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Adsorption</term><term>Anal</term><term>Aqueous solution</term><term>Avidin</term><term>Bead</term><term>Bead conjugates</term><term>Beads</term><term>Binding isotherms</term><term>Binding sites</term><term>Bovine serum albumin</term><term>Carrier buffer</term><term>Carrier solution</term><term>Chem</term><term>Cleavable crosslinker</term><term>Compact layer</term><term>Electrical charge</term><term>Electropolymerization</term><term>Full paper</term><term>Funct</term><term>Gmbh</term><term>Heterobifunctional crosslinker</term><term>Imprinting</term><term>Imprinting factor</term><term>Kgaa</term><term>Lithography</term><term>Macromolecular template</term><term>Mater</term><term>Mips</term><term>Nanogravimetric measurements</term><term>Nanosphere</term><term>Nanosphere lithography</term><term>Polymer</term><term>Polymer surface</term><term>Polystyrene beads</term><term>Preferential growth</term><term>Protein imprinting</term><term>Protein target</term><term>Quartz</term><term>Quartz crystal resonator</term><term>Quartz crystals</term><term>Selective protein recognition</term><term>Sigma aldrich</term><term>Successive steps</term><term>Target molecule</term><term>Verlag</term><term>Verlag gmbh</term><term>Weinheim</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A versatile approach based on nanosphere lithography is proposed to generate surface‐imprinted polymers for selective protein recognition. A layer of 750 nm diameter latex bead‐protein conjugate is deposited onto the surface of gold‐coated quartz crystals followed by the electrosynthesis of a poly(3,4‐ethylenedioxythiophene)/poly(styrenesulfonate) (PEDOT/PSS) film with thicknesses on the order of the bead radius. The removal of the polymer bead‐protein conjugates, facilitated by using a cleavable protein‐nanosphere linkage is shown to result in 2D arrays of periodic complementary size cavities. Here it is demonstrated by nanogravimetric measurements that the imprinting proceeds further at molecular level and the protein (avidin) coating of the beads generates selective recognition sites for avidin on the surface of the PEDOT/PSS film. The binding capacity of such surface‐imprinted polymer films is ca. 6.5 times higher than that of films imprinted with unmodified beads. They also exhibit excellent selectivity against analogues of avidin, i.e., extravidin, streptavidin, and neutravidin, the latter being in fact undetectable. This methodology, if coupled with properly oriented conjugation of the macromolecular template to the nanoparticles, offers the possibility of site‐directed imprinting.</div><div type="abstract" xml:lang="en">A versatile approach based on nanosphere lithography is proposed to generate surface‐imprinted polymers for selective protein recognition. Nanogravimetric measurements demonstrate that the protein (avidin) coating of the nanospheres generates selective recognition sites for avidin on the surface of the PEDOT/PSS film. This methodology coupled with oriented conjugation of the macromolecular template to the nanospheres offers the possibility of site‐directed imprinting.</div></front></TEI><affiliations><list><country><li>Hongrie</li></country></list><tree><country name="Hongrie"><noRegion><name sortKey="Bognar, Julia" sort="Bognar, Julia" uniqKey="Bognar J" first="Júlia" last="Bognár">Júlia Bognár</name></noRegion><name sortKey="Dork, Zsanett" sort="Dork, Zsanett" uniqKey="Dork Z" first="Zsanett" last="Dork">Zsanett Dork</name><name sortKey="Gyurcsanyi, R Bert E" sort="Gyurcsanyi, R Bert E" uniqKey="Gyurcsanyi R" first="R Bert E." last="Gyurcsányi">R Bert E. Gyurcsányi</name><name sortKey="Gyurcsanyi, R Bert E" sort="Gyurcsanyi, R Bert E" uniqKey="Gyurcsanyi R" first="R Bert E." last="Gyurcsányi">R Bert E. Gyurcsányi</name><name sortKey="Gyurcsanyi, R Bert E" sort="Gyurcsanyi, R Bert E" uniqKey="Gyurcsanyi R" first="R Bert E." last="Gyurcsányi">R Bert E. Gyurcsányi</name><name sortKey="Gyurcsanyi, R Bert E" sort="Gyurcsanyi, R Bert E" uniqKey="Gyurcsanyi R" first="R Bert E." last="Gyurcsányi">R Bert E. Gyurcsányi</name><name sortKey="Horvath, Viola" sort="Horvath, Viola" uniqKey="Horvath V" first="Viola" last="Horváth">Viola Horváth</name><name sortKey="Sz Cs, Julia" sort="Sz Cs, Julia" uniqKey="Sz Cs J" first="Júlia" last="Sz Cs">Júlia Sz Cs</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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