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Electrochemical Biosensors Based on Membrane-Bound Enzymes in Biomimetic Configurations
In nature, many enzymes are attached or inserted into the cell membrane, having hydrophobic subunits or lipid chains for this purpose. Their reconstitution on electrodes maintaining their natural structural characteristics allows for optimizing their electrocatalytic properties and stability. Differ...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7349357/ https://www.ncbi.nlm.nih.gov/pubmed/32560121 http://dx.doi.org/10.3390/s20123393 |
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author | Alvarez-Malmagro, Julia García-Molina, Gabriel López De Lacey, Antonio |
author_facet | Alvarez-Malmagro, Julia García-Molina, Gabriel López De Lacey, Antonio |
author_sort | Alvarez-Malmagro, Julia |
collection | PubMed |
description | In nature, many enzymes are attached or inserted into the cell membrane, having hydrophobic subunits or lipid chains for this purpose. Their reconstitution on electrodes maintaining their natural structural characteristics allows for optimizing their electrocatalytic properties and stability. Different biomimetic strategies have been developed for modifying electrodes surfaces to accommodate membrane-bound enzymes, including the formation of self-assembled monolayers of hydrophobic compounds, lipid bilayers, or liposomes deposition. An overview of the different strategies used for the formation of biomimetic membranes, the reconstitution of membrane enzymes on electrodes, and their applications as biosensors is presented. |
format | Online Article Text |
id | pubmed-7349357 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-73493572020-07-22 Electrochemical Biosensors Based on Membrane-Bound Enzymes in Biomimetic Configurations Alvarez-Malmagro, Julia García-Molina, Gabriel López De Lacey, Antonio Sensors (Basel) Review In nature, many enzymes are attached or inserted into the cell membrane, having hydrophobic subunits or lipid chains for this purpose. Their reconstitution on electrodes maintaining their natural structural characteristics allows for optimizing their electrocatalytic properties and stability. Different biomimetic strategies have been developed for modifying electrodes surfaces to accommodate membrane-bound enzymes, including the formation of self-assembled monolayers of hydrophobic compounds, lipid bilayers, or liposomes deposition. An overview of the different strategies used for the formation of biomimetic membranes, the reconstitution of membrane enzymes on electrodes, and their applications as biosensors is presented. MDPI 2020-06-16 /pmc/articles/PMC7349357/ /pubmed/32560121 http://dx.doi.org/10.3390/s20123393 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Alvarez-Malmagro, Julia García-Molina, Gabriel López De Lacey, Antonio Electrochemical Biosensors Based on Membrane-Bound Enzymes in Biomimetic Configurations |
title | Electrochemical Biosensors Based on Membrane-Bound Enzymes in Biomimetic Configurations |
title_full | Electrochemical Biosensors Based on Membrane-Bound Enzymes in Biomimetic Configurations |
title_fullStr | Electrochemical Biosensors Based on Membrane-Bound Enzymes in Biomimetic Configurations |
title_full_unstemmed | Electrochemical Biosensors Based on Membrane-Bound Enzymes in Biomimetic Configurations |
title_short | Electrochemical Biosensors Based on Membrane-Bound Enzymes in Biomimetic Configurations |
title_sort | electrochemical biosensors based on membrane-bound enzymes in biomimetic configurations |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7349357/ https://www.ncbi.nlm.nih.gov/pubmed/32560121 http://dx.doi.org/10.3390/s20123393 |
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