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Capacitance-modulated transistor detects odorant binding protein chiral interactions
Peripheral events in olfaction involve odorant binding proteins (OBPs) whose role in the recognition of different volatile chemicals is yet unclear. Here we report on the sensitive and quantitative measurement of the weak interactions associated with neutral enantiomers differentially binding to OBP...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4309438/ https://www.ncbi.nlm.nih.gov/pubmed/25591754 http://dx.doi.org/10.1038/ncomms7010 |
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author | Mulla, Mohammad Yusuf Tuccori, Elena Magliulo, Maria Lattanzi, Gianluca Palazzo, Gerardo Persaud, Krishna Torsi, Luisa |
author_facet | Mulla, Mohammad Yusuf Tuccori, Elena Magliulo, Maria Lattanzi, Gianluca Palazzo, Gerardo Persaud, Krishna Torsi, Luisa |
author_sort | Mulla, Mohammad Yusuf |
collection | PubMed |
description | Peripheral events in olfaction involve odorant binding proteins (OBPs) whose role in the recognition of different volatile chemicals is yet unclear. Here we report on the sensitive and quantitative measurement of the weak interactions associated with neutral enantiomers differentially binding to OBPs immobilized through a self-assembled monolayer to the gate of an organic bio-electronic transistor. The transduction is remarkably sensitive as the transistor output current is governed by the small capacitance of the protein layer undergoing minute changes as the ligand–protein complex is formed. Accurate determination of the free-energy balances and of the capacitance changes associated with the binding process allows derivation of the free-energy components as well as of the occurrence of conformational events associated with OBP ligand binding. Capacitance-modulated transistors open a new pathway for the study of ultra-weak molecular interactions in surface-bound protein–ligand complexes through an approach that combines bio-chemical and electronic thermodynamic parameters. |
format | Online Article Text |
id | pubmed-4309438 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Pub. Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-43094382015-02-09 Capacitance-modulated transistor detects odorant binding protein chiral interactions Mulla, Mohammad Yusuf Tuccori, Elena Magliulo, Maria Lattanzi, Gianluca Palazzo, Gerardo Persaud, Krishna Torsi, Luisa Nat Commun Article Peripheral events in olfaction involve odorant binding proteins (OBPs) whose role in the recognition of different volatile chemicals is yet unclear. Here we report on the sensitive and quantitative measurement of the weak interactions associated with neutral enantiomers differentially binding to OBPs immobilized through a self-assembled monolayer to the gate of an organic bio-electronic transistor. The transduction is remarkably sensitive as the transistor output current is governed by the small capacitance of the protein layer undergoing minute changes as the ligand–protein complex is formed. Accurate determination of the free-energy balances and of the capacitance changes associated with the binding process allows derivation of the free-energy components as well as of the occurrence of conformational events associated with OBP ligand binding. Capacitance-modulated transistors open a new pathway for the study of ultra-weak molecular interactions in surface-bound protein–ligand complexes through an approach that combines bio-chemical and electronic thermodynamic parameters. Nature Pub. Group 2015-01-16 /pmc/articles/PMC4309438/ /pubmed/25591754 http://dx.doi.org/10.1038/ncomms7010 Text en Copyright © 2015, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Mulla, Mohammad Yusuf Tuccori, Elena Magliulo, Maria Lattanzi, Gianluca Palazzo, Gerardo Persaud, Krishna Torsi, Luisa Capacitance-modulated transistor detects odorant binding protein chiral interactions |
title | Capacitance-modulated transistor detects odorant binding protein chiral interactions |
title_full | Capacitance-modulated transistor detects odorant binding protein chiral interactions |
title_fullStr | Capacitance-modulated transistor detects odorant binding protein chiral interactions |
title_full_unstemmed | Capacitance-modulated transistor detects odorant binding protein chiral interactions |
title_short | Capacitance-modulated transistor detects odorant binding protein chiral interactions |
title_sort | capacitance-modulated transistor detects odorant binding protein chiral interactions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4309438/ https://www.ncbi.nlm.nih.gov/pubmed/25591754 http://dx.doi.org/10.1038/ncomms7010 |
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