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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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 |
work_keys_str_mv |
AT flexerv structureandthicknessdependenceofmolecularwiringinnanostructuredenzymemultilayers AT forzanies structureandthicknessdependenceofmolecularwiringinnanostructuredenzymemultilayers AT calvoej structureandthicknessdependenceofmolecularwiringinnanostructuredenzymemultilayers AT luduenasj structureandthicknessdependenceofmolecularwiringinnanostructuredenzymemultilayers AT pietrasantali structureandthicknessdependenceofmolecularwiringinnanostructuredenzymemultilayers |
_version_ |
1807319840246988800 |