Structure and thickness dependence of "molecular wiring" in nanostructured enzyme multilayers

Supramolecular organized multilayers composed of glucose oxidase (GOx) and osmium-derivatized poly(allylamine) redox polymer have been self-assembled electrostatically from Os-polyelectrolyte solutions of variable pH (5.5-8.8) leading to a decrease of the linear charge density in the PAH-Os with inc...

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Autores principales: Flexer, V., Forzani, E.S., Calvo, E.J., Ludueña, S.J., Pietrasanta, L.I.
Formato: JOUR
Materias:
AFM
pH
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00032700_v78_n2_p399_Flexer
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spelling todo:paper_00032700_v78_n2_p399_Flexer2023-10-03T13:56:02Z Structure and thickness dependence of "molecular wiring" in nanostructured enzyme multilayers Flexer, V. Forzani, E.S. Calvo, E.J. Ludueña, S.J. Pietrasanta, L.I. AFM Electrocatalytic oxidation Glucose oxidase (GOx) Quartz crystal microbalance Adsorption Cyclic voltammetry Ellipsometry Nanostructured materials Oxidation Polymers Quartz applications Structural analysis Enzyme kinetics allylamine bipyridine derivative glucose glucose oxidase nanoparticle osmium derivative polyallylamine polyelectrolyte silicon dioxide unclassified drug adsorption article atomic force microscopy catalysis cyclic potentiometry electrode ellipsometry enzyme electrode enzyme structure film oxidation oxidation reduction reaction pH supramolecular chemistry thickness Electrochemistry Glucose Glucose Oxidase Microscopy, Atomic Force Nanostructures Organometallic Compounds Osmium Oxidation-Reduction Polyamines Supramolecular organized multilayers composed of glucose oxidase (GOx) and osmium-derivatized poly(allylamine) redox polymer have been self-assembled electrostatically from Os-polyelectrolyte solutions of variable pH (5.5-8.8) leading to a decrease of the linear charge density in the PAH-Os with increasing pH. The layer-by-layer enzyme multilayers were studied by ellipsometry, quartz crystal microbalance, AFM, cyclic voltammetry, and electrocatalytic oxidation of β-D-glucose. At higher adsorption solution pH, an increase in the film thickness, enzyme loading, and redox charge was observed. While the electrocatalytic response increases with the increase of the adsorption solution pH (decrease of the polyelectrolyte linear charge), the FADH2 oxidation bimolecular rate constant has a maximum in the pH range 7.0-7.5 where a change in the film growth mechanism is observed. © 2006 American Chemical Society. Fil:Flexer, V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Calvo, E.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00032700_v78_n2_p399_Flexer
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic AFM
Electrocatalytic oxidation
Glucose oxidase (GOx)
Quartz crystal microbalance
Adsorption
Cyclic voltammetry
Ellipsometry
Nanostructured materials
Oxidation
Polymers
Quartz applications
Structural analysis
Enzyme kinetics
allylamine
bipyridine derivative
glucose
glucose oxidase
nanoparticle
osmium derivative
polyallylamine
polyelectrolyte
silicon dioxide
unclassified drug
adsorption
article
atomic force microscopy
catalysis
cyclic potentiometry
electrode
ellipsometry
enzyme electrode
enzyme structure
film
oxidation
oxidation reduction reaction
pH
supramolecular chemistry
thickness
Electrochemistry
Glucose
Glucose Oxidase
Microscopy, Atomic Force
Nanostructures
Organometallic Compounds
Osmium
Oxidation-Reduction
Polyamines
spellingShingle AFM
Electrocatalytic oxidation
Glucose oxidase (GOx)
Quartz crystal microbalance
Adsorption
Cyclic voltammetry
Ellipsometry
Nanostructured materials
Oxidation
Polymers
Quartz applications
Structural analysis
Enzyme kinetics
allylamine
bipyridine derivative
glucose
glucose oxidase
nanoparticle
osmium derivative
polyallylamine
polyelectrolyte
silicon dioxide
unclassified drug
adsorption
article
atomic force microscopy
catalysis
cyclic potentiometry
electrode
ellipsometry
enzyme electrode
enzyme structure
film
oxidation
oxidation reduction reaction
pH
supramolecular chemistry
thickness
Electrochemistry
Glucose
Glucose Oxidase
Microscopy, Atomic Force
Nanostructures
Organometallic Compounds
Osmium
Oxidation-Reduction
Polyamines
Flexer, V.
Forzani, E.S.
Calvo, E.J.
Ludueña, S.J.
Pietrasanta, L.I.
Structure and thickness dependence of "molecular wiring" in nanostructured enzyme multilayers
topic_facet AFM
Electrocatalytic oxidation
Glucose oxidase (GOx)
Quartz crystal microbalance
Adsorption
Cyclic voltammetry
Ellipsometry
Nanostructured materials
Oxidation
Polymers
Quartz applications
Structural analysis
Enzyme kinetics
allylamine
bipyridine derivative
glucose
glucose oxidase
nanoparticle
osmium derivative
polyallylamine
polyelectrolyte
silicon dioxide
unclassified drug
adsorption
article
atomic force microscopy
catalysis
cyclic potentiometry
electrode
ellipsometry
enzyme electrode
enzyme structure
film
oxidation
oxidation reduction reaction
pH
supramolecular chemistry
thickness
Electrochemistry
Glucose
Glucose Oxidase
Microscopy, Atomic Force
Nanostructures
Organometallic Compounds
Osmium
Oxidation-Reduction
Polyamines
description Supramolecular organized multilayers composed of glucose oxidase (GOx) and osmium-derivatized poly(allylamine) redox polymer have been self-assembled electrostatically from Os-polyelectrolyte solutions of variable pH (5.5-8.8) leading to a decrease of the linear charge density in the PAH-Os with increasing pH. The layer-by-layer enzyme multilayers were studied by ellipsometry, quartz crystal microbalance, AFM, cyclic voltammetry, and electrocatalytic oxidation of β-D-glucose. At higher adsorption solution pH, an increase in the film thickness, enzyme loading, and redox charge was observed. While the electrocatalytic response increases with the increase of the adsorption solution pH (decrease of the polyelectrolyte linear charge), the FADH2 oxidation bimolecular rate constant has a maximum in the pH range 7.0-7.5 where a change in the film growth mechanism is observed. © 2006 American Chemical Society.
format JOUR
author Flexer, V.
Forzani, E.S.
Calvo, E.J.
Ludueña, S.J.
Pietrasanta, L.I.
author_facet Flexer, V.
Forzani, E.S.
Calvo, E.J.
Ludueña, S.J.
Pietrasanta, L.I.
author_sort Flexer, V.
title Structure and thickness dependence of "molecular wiring" in nanostructured enzyme multilayers
title_short Structure and thickness dependence of "molecular wiring" in nanostructured enzyme multilayers
title_full Structure and thickness dependence of "molecular wiring" in nanostructured enzyme multilayers
title_fullStr Structure and thickness dependence of "molecular wiring" in nanostructured enzyme multilayers
title_full_unstemmed Structure and thickness dependence of "molecular wiring" in nanostructured enzyme multilayers
title_sort structure and thickness dependence of "molecular wiring" in nanostructured enzyme multilayers
url http://hdl.handle.net/20.500.12110/paper_00032700_v78_n2_p399_Flexer
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AT luduenasj structureandthicknessdependenceofmolecularwiringinnanostructuredenzymemultilayers
AT pietrasantali structureandthicknessdependenceofmolecularwiringinnanostructuredenzymemultilayers
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