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Human olfactory receptor 17-40 as an active part of a nanobiosensor: a microscopic investigation of its electrical properties

Title: Human olfactory receptor 17-40 as an active part of a nanobiosensor: a microscopic investigation of its electrical properties
Authors: Alfinito, Eleonora; Millithaler, Jean-Francois; Reggiani, Lino; Zine, Nadia; Jaffrezic-Renault, Nicole
Contributors: Dipartimento di Ingegneria dell'Innovazione; Università del Salento = University of Salento Lecce; Consorzio Nazl Interuniv Sci Fis Mat (CNISM); CNISM; SIMS - Surfaces-(bio)Interfaces - Micro & Nano Systèmes (2011-2014); Institut des Sciences Analytiques (ISA); Université Claude Bernard Lyon 1 (UCBL); Université de Lyon-Université de Lyon-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL); Université de Lyon-Université de Lyon-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS); the bioelectronic olfactory neuron device (BOND) project CE within the 7th Program, grant agreement: 228685-2; European Project
Source: ISSN: 2046-2069 ; RSC Advances ; https://hal.science/hal-00809719 ; RSC Advances, 2011, 1 (1), pp.123-127. ⟨10.1039/c1ra00025j⟩.
Publisher Information: CCSD; Royal Society of Chemistry
Publication Year: 2011
Collection: HAL Lyon 1 (University Claude Bernard Lyon 1)
Subject Terms: BIOELECTRONIC NOSE; ODORANT-RECEPTOR; BIOSENSOR; OR17-40; [CHIM.ANAL]Chemical Sciences/Analytical chemistry
Description: International audience ; Increasing attention has recently been devoted to protein-based nanobiosensors. The main reason is the huge number of possible technological applications, ranging from drug detection to early cancer diagnosis. Their operating model is based on protein activation and the corresponding conformational change due to the capture of an external molecule, the so-called ligand. Recent measurements, performed with different techniques on the human 17-40 olfactory receptor, revealed a very narrow window of response in respect to the odour concentration. This is a crucial point for understanding whether the use of this olfactory receptor as a sensitive part of a nanobiosensor is a good choice. In this paper we investigate the topological and electrical properties of the human olfactory receptor 17-40 with the objective of providing a microscopic interpretation of available experiments. To this purpose, we model the protein by means of a graph that is able to capture the mean features of the 3D backbone structure. The graph is then associated with an equivalent impedance network, able to evaluate the impedance spectra of the olfactory receptor in its native and activated state. We assume a topological origin of the different protein electrical responses to different ligand concentrations: In this perspective all the experimental data are collected and interpreted satisfactorily within a unified scheme, also useful for application to other proteins.
Document Type: article in journal/newspaper
Language: English
Relation: info:eu-repo/semantics/altIdentifier/arxiv/1107.2778; ARXIV: 1107.2778
DOI: 10.1039/c1ra00025j
Availability: https://hal.science/hal-00809719; https://doi.org/10.1039/c1ra00025j
Accession Number: edsbas.826D5218
Database: BASE