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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.
Afiliação
  • Larisika M; BioSensor Technologies, Austrian Institute of Technology, Vienna (Austria).
  • Kotlowski C; Centre for Biomimetic Sensor Science, Nanyang Technological University, Singapore 637371 (Singapore).
  • Steininger C; BioSensor Technologies, Austrian Institute of Technology, Vienna (Austria).
  • Mastrogiacomo R; Center for Electrochemical Surface Technology, Wiener Neustadt (Austria).
  • Pelosi P; BioSensor Technologies, Austrian Institute of Technology, Vienna (Austria).
  • Schütz S; Department of Biology of Agriculture, Food and Environment, University of Pisa (Italy).
  • Peteu SF; Department of Biology of Agriculture, Food and Environment, University of Pisa (Italy).
  • Kleber C; Buesgen-Institute, Dept. of Forest Zoology and Forest Conservation, Goettingen (Germany).
  • Reiner-Rozman C; Michigan State University, Chemical Engineering & Materials Science (USA).
  • Nowak C; Center for Electrochemical Surface Technology, Wiener Neustadt (Austria).
  • Knoll W; BioSensor Technologies, Austrian Institute of Technology, Vienna (Austria).
Angew Chem Int Ed Engl ; 54(45): 13245-8, 2015 Nov 02.
Article em En | MEDLINE | ID: mdl-26364873
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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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Óxidos / Transistores Eletrônicos / Abelhas / Técnicas Biossensoriais / Receptores Odorantes / Grafite / Odorantes Limite: Animals Idioma: En Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Óxidos / Transistores Eletrônicos / Abelhas / Técnicas Biossensoriais / Receptores Odorantes / Grafite / Odorantes Limite: Animals Idioma: En Ano de publicação: 2015 Tipo de documento: Article