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Electronic Olfactory Sensor Based on A. mellifera Odorant‐Binding Protein 14 on a Reduced Graphene Oxide Field‐Effect Transistor

An olfactory biosensor based on a reduced graphene oxide (rGO) field‐effect transistor (FET), functionalized by the odorant‐binding protein 14 (OBP14) from the honey bee (Apis mellifera) has been designed for the in situ and real‐time monitoring of a broad spectrum of odorants in aqueous solutions k...

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Autores principales: Larisika, Melanie, Kotlowski, Caroline, Steininger, Christoph, Mastrogiacomo, Rosa, Pelosi, Paolo, Schütz, Stefan, Peteu, Serban F., Kleber, Christoph, Reiner‐Rozman, Ciril, Nowak, Christoph, Knoll, Wolfgang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY‐VCH Verlag 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4768645/
https://www.ncbi.nlm.nih.gov/pubmed/26364873
http://dx.doi.org/10.1002/anie.201505712
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author Larisika, Melanie
Kotlowski, Caroline
Steininger, Christoph
Mastrogiacomo, Rosa
Pelosi, Paolo
Schütz, Stefan
Peteu, Serban F.
Kleber, Christoph
Reiner‐Rozman, Ciril
Nowak, Christoph
Knoll, Wolfgang
author_facet Larisika, Melanie
Kotlowski, Caroline
Steininger, Christoph
Mastrogiacomo, Rosa
Pelosi, Paolo
Schütz, Stefan
Peteu, Serban F.
Kleber, Christoph
Reiner‐Rozman, Ciril
Nowak, Christoph
Knoll, Wolfgang
author_sort Larisika, Melanie
collection PubMed
description An olfactory biosensor based on a reduced graphene oxide (rGO) field‐effect transistor (FET), functionalized by the odorant‐binding protein 14 (OBP14) from the honey bee (Apis mellifera) has been designed for the in situ and real‐time monitoring of a broad spectrum of odorants in aqueous solutions known to be attractants for bees. The electrical measurements of the binding of all tested odorants are shown to follow the Langmuir model for ligand–receptor interactions. The results demonstrate that OBP14 is able to bind odorants even after immobilization on rGO and can discriminate between ligands binding within a range of dissociation constants from K (d)=4 μm to K (d)=3.3 mm. The strongest ligands, such as homovanillic acid, eugenol, and methyl vanillate all contain a hydroxy group which is apparently important for the strong interaction with the protein.
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spelling pubmed-47686452016-03-09 Electronic Olfactory Sensor Based on A. mellifera Odorant‐Binding Protein 14 on a Reduced Graphene Oxide Field‐Effect Transistor Larisika, Melanie Kotlowski, Caroline Steininger, Christoph Mastrogiacomo, Rosa Pelosi, Paolo Schütz, Stefan Peteu, Serban F. Kleber, Christoph Reiner‐Rozman, Ciril Nowak, Christoph Knoll, Wolfgang Angew Chem Int Ed Engl Communications An olfactory biosensor based on a reduced graphene oxide (rGO) field‐effect transistor (FET), functionalized by the odorant‐binding protein 14 (OBP14) from the honey bee (Apis mellifera) has been designed for the in situ and real‐time monitoring of a broad spectrum of odorants in aqueous solutions known to be attractants for bees. The electrical measurements of the binding of all tested odorants are shown to follow the Langmuir model for ligand–receptor interactions. The results demonstrate that OBP14 is able to bind odorants even after immobilization on rGO and can discriminate between ligands binding within a range of dissociation constants from K (d)=4 μm to K (d)=3.3 mm. The strongest ligands, such as homovanillic acid, eugenol, and methyl vanillate all contain a hydroxy group which is apparently important for the strong interaction with the protein. WILEY‐VCH Verlag 2015-09-14 2015-11-02 /pmc/articles/PMC4768645/ /pubmed/26364873 http://dx.doi.org/10.1002/anie.201505712 Text en © 2015 The Authors. Published by Wiley‐VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. Open access.
spellingShingle Communications
Larisika, Melanie
Kotlowski, Caroline
Steininger, Christoph
Mastrogiacomo, Rosa
Pelosi, Paolo
Schütz, Stefan
Peteu, Serban F.
Kleber, Christoph
Reiner‐Rozman, Ciril
Nowak, Christoph
Knoll, Wolfgang
Electronic Olfactory Sensor Based on A. mellifera Odorant‐Binding Protein 14 on a Reduced Graphene Oxide Field‐Effect Transistor
title Electronic Olfactory Sensor Based on A. mellifera Odorant‐Binding Protein 14 on a Reduced Graphene Oxide Field‐Effect Transistor
title_full Electronic Olfactory Sensor Based on A. mellifera Odorant‐Binding Protein 14 on a Reduced Graphene Oxide Field‐Effect Transistor
title_fullStr Electronic Olfactory Sensor Based on A. mellifera Odorant‐Binding Protein 14 on a Reduced Graphene Oxide Field‐Effect Transistor
title_full_unstemmed Electronic Olfactory Sensor Based on A. mellifera Odorant‐Binding Protein 14 on a Reduced Graphene Oxide Field‐Effect Transistor
title_short Electronic Olfactory Sensor Based on A. mellifera Odorant‐Binding Protein 14 on a Reduced Graphene Oxide Field‐Effect Transistor
title_sort electronic olfactory sensor based on a. mellifera odorant‐binding protein 14 on a reduced graphene oxide field‐effect transistor
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4768645/
https://www.ncbi.nlm.nih.gov/pubmed/26364873
http://dx.doi.org/10.1002/anie.201505712
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