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dc.creatorCortez, María Lorena-
dc.creatorPallarola, Diego Andres-
dc.creatorCeolin, Marcelo Raul-
dc.creatorAzzaroni, Omar-
dc.creatorBattaglini, Fernando-
dc.date2016-04-11T21:03:13Z-
dc.date2016-04-11T21:03:13Z-
dc.date2013-02-
dc.date2016-05-06 15:52:43.262787-03-
dc.date.accessioned2019-04-29T15:53:49Z-
dc.date.available2019-04-29T15:53:49Z-
dc.date.issued2013-02-
dc.identifierCortez, María Lorena; Pallarola, Diego Andres; Ceolin, Marcelo Raul; Azzaroni, Omar; Battaglini, Fernando; Electron Transfer Properties of Dual Self-Assembled Architectures Based on Specific Recognition and Electrostatic Driving Forces: Its Application To Control Substrate Inhibition in Horseradish Peroxidase-Based Sensors; American Chemical Society; Analytical Chemistry; 85; 4; 2-2013; 2414-2422-
dc.identifier0003-2700-
dc.identifierhttp://hdl.handle.net/11336/5137-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/304919-
dc.descriptionThis work describes the synergistic combination of ionic self-assembly and recognition-directed assembly with the aim of creating highly functional bioelectrochemical interfaces compatible with the supramolecular design of a wide variety of biosensing platforms. A recently synthesized glycopolyelectrolyte constituted of polyallylamine bearing redox-active osmium complexes and glycosidic residues (lactose) is used to create a self-assembled structure with sodium dodecylsulfate. In turn, this supramolecular thin films bearing redox-active and biorecognizable carbohydrate units enable the facile assembly of functional lectins as well as the subsequent docking and "wiring" of glycoenzymes, like horseradish peroxidase (HRP) (an elusive enzyme to immobilize via noncovalent interactions). The assembly of this system was followed by quartz crystal microbalance and grazingincidence small-angle X-ray scattering (GISAXS) studies confirming that spin-coated ionically self-assembled films exhibit mesostructured architectures according to the formation of self-organized lamellar structures. In-depth characterization of the electrocatalytic properties of the biosupramacromolecular assemblies confirmed the ability of this kind of interfacial architecture to efficiently mediate electron transfer processes between the glycoenzyme and the electrode surface. For instance, our experimental electrochemical evidence clearly shows that tailor-made interfacial configurations of the ionic self-assemblies can prevent the inhibition of the glycoenzyme (typically observed in HRP) leading to bioelectrocatalytic currents up to 0.1 mA cm−2. The presence of carbohydrate moieties in the ionic domains promotes the biorecognition-driven assembly of lectins adding a new dimension to the capabilities of ionic self-assembly.-
dc.descriptionFil: Cortez, María Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina-
dc.descriptionFil: Pallarola, Diego Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Universidad Nacional de La Plata; Argentina-
dc.descriptionFil: Ceolin, Marcelo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Universidad Nacional de La Plata; Argentina-
dc.descriptionFil: Azzaroni, Omar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Universidad Nacional de La Plata; Argentina-
dc.descriptionFil: Battaglini, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina-
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dc.languageeng-
dc.publisherAmerican Chemical Society-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/ac303424t-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/10.1021/ac303424t-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/ac303424t-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectELECTRON TRANSFER-
dc.subjectSIGNAL TRANSDUCTION-
dc.subjectSOFT MATTER-
dc.subjectFísico-Química, Ciencia de los Polímeros, Electroquímica-
dc.subjectCiencias Químicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleElectron Transfer Properties of Dual Self-Assembled Architectures Based on Specific Recognition and Electrostatic Driving Forces: Its Application To Control Substrate Inhibition in Horseradish Peroxidase-Based Sensors-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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