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Nanobioengineering and Characterization of a Novel Estrogen Receptor Biosensor

We constructed an original supramolecular assembly on a surface of sensor composed of an innovative combination of an engineered cytochrome b5 and a modified nucleic acid bound to a synthetic lipid hemimembrane. The protein/DNA block, called (P-DNA)(2), was synthesized and purified before its immobi...

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Detalles Bibliográficos
Autores principales: Berthier, Alexandre, Elie-Caille, Céline, Lesniewska, Eric, Delage-Mourroux, Régis, Boireau, Wilfrid
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3697183/
https://www.ncbi.nlm.nih.gov/pubmed/27879944
http://dx.doi.org/10.3390/s8074413
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author Berthier, Alexandre
Elie-Caille, Céline
Lesniewska, Eric
Delage-Mourroux, Régis
Boireau, Wilfrid
author_facet Berthier, Alexandre
Elie-Caille, Céline
Lesniewska, Eric
Delage-Mourroux, Régis
Boireau, Wilfrid
author_sort Berthier, Alexandre
collection PubMed
description We constructed an original supramolecular assembly on a surface of sensor composed of an innovative combination of an engineered cytochrome b5 and a modified nucleic acid bound to a synthetic lipid hemimembrane. The protein/DNA block, called (P-DNA)(2), was synthesized and purified before its immobilization onto a hybrid bilayer reconstituted on a gold surface. Surface plasmon resonance (SPR) and atomic force microscopy (AFM) were engaged in parallel on the same substrates in order to better understand dynamic events that occur at the surface of the biosensor. Good correlations were obtained in terms of specificity and reversibility. These findings allow us to present a first application of such biosensor in the study of the interaction processes between nuclear receptor and DNA.
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spelling pubmed-36971832013-07-01 Nanobioengineering and Characterization of a Novel Estrogen Receptor Biosensor Berthier, Alexandre Elie-Caille, Céline Lesniewska, Eric Delage-Mourroux, Régis Boireau, Wilfrid Sensors (Basel) Article We constructed an original supramolecular assembly on a surface of sensor composed of an innovative combination of an engineered cytochrome b5 and a modified nucleic acid bound to a synthetic lipid hemimembrane. The protein/DNA block, called (P-DNA)(2), was synthesized and purified before its immobilization onto a hybrid bilayer reconstituted on a gold surface. Surface plasmon resonance (SPR) and atomic force microscopy (AFM) were engaged in parallel on the same substrates in order to better understand dynamic events that occur at the surface of the biosensor. Good correlations were obtained in terms of specificity and reversibility. These findings allow us to present a first application of such biosensor in the study of the interaction processes between nuclear receptor and DNA. Molecular Diversity Preservation International (MDPI) 2008-07-28 /pmc/articles/PMC3697183/ /pubmed/27879944 http://dx.doi.org/10.3390/s8074413 Text en © 2008 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Berthier, Alexandre
Elie-Caille, Céline
Lesniewska, Eric
Delage-Mourroux, Régis
Boireau, Wilfrid
Nanobioengineering and Characterization of a Novel Estrogen Receptor Biosensor
title Nanobioengineering and Characterization of a Novel Estrogen Receptor Biosensor
title_full Nanobioengineering and Characterization of a Novel Estrogen Receptor Biosensor
title_fullStr Nanobioengineering and Characterization of a Novel Estrogen Receptor Biosensor
title_full_unstemmed Nanobioengineering and Characterization of a Novel Estrogen Receptor Biosensor
title_short Nanobioengineering and Characterization of a Novel Estrogen Receptor Biosensor
title_sort nanobioengineering and characterization of a novel estrogen receptor biosensor
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3697183/
https://www.ncbi.nlm.nih.gov/pubmed/27879944
http://dx.doi.org/10.3390/s8074413
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