Monoamine oxidase B layer-by-layer film fabrication and characterization toward dopamine detection

Monoamine oxidase B layer-by-layer film fabrication and characterization toward dopamine detection

Author Miyazaki, Celina Massumi Google Scholar
Pereira, Tamyris Paschoal Google Scholar
Tavares Mascagni, Daniela Branco Google Scholar
de Moraes, Marli Leite Autor UNIFESP Google Scholar
Ferreira, Marystela Google Scholar
Abstract In this work nanostructured film composites of the monoamine oxidase B (MAO-B) enzyme, free or encapsulated in liposomes, were fabricated by the layer-by-layer (LbL) self-assembly technique, employing polyethylene imine (PEI) as polycation. Initially, the MAO-B enzyme was incorporated into liposomes in order to preserve its enzymatic structure ensuring their activity and catalytic stability. The LbL film growth was monitored by surface plasmon resonance (SPR) by gold resonance angle shift analysis after each bilayer deposition. Subsequently, the films were applied as amperometric biosensors for dopamine detection using Prussian Blue (PB) as the electron mediator. The biosensor fabricated by MAO-B incorporated into liposomes composed of DPPG:POPG in the ratio (1:4) (w/w) showed the best performance with a sensitivity of 0.86 (mu A cm(-2))/(mmol L-1) and a detection limit of 033 mmol L-1. (C) 2015 Elsevier B.V. All rights reserved.
Keywords Layer-by-layer
Monoamine oxidase-B
Dopamine detection
AmperometryAssembled Multilayer Films
Tandem Mass-Spectrometry
Carbon Nanotubes
Electrochemical Sensors
Hemoglobin Immobilization
Amperometric Biosensors
Language English
Sponsor Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Grant number FAPESP: 2014/15093-7
FAPESP: 2014/17519-1
Date 2016
Published in Materials Science & Engineering C-Materials For Biological Applications. Amsterdam, v. 58, p. 310-315, 2016.
ISSN 0928-4931 (Sherpa/Romeo, impact factor)
Publisher Elsevier Science Bv
Extent 310-315
Access rights Closed access
Type Article
Web of Science ID WOS:000364247500036

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