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Printed-Circuit-Board-Based Two-Electrode System for Electronic Characterization of Proteins

[Image: see text] Proteins have been increasingly suggested as suitable candidates for the fabrication of biological computers and other biomolecular-based electronic devices mainly due to their interesting structure-related intrinsic electrical properties. These natural biopolymers are environmenta...

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Autores principales: Talebi, Sara, Daraghma, Souhad M. A., Subramaniam, Ramesh T., Bhassu, Subha, Gnana Kumar, Georgepeter, Periasamy, Vengadesh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7160841/
https://www.ncbi.nlm.nih.gov/pubmed/32309689
http://dx.doi.org/10.1021/acsomega.9b03831
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author Talebi, Sara
Daraghma, Souhad M. A.
Subramaniam, Ramesh T.
Bhassu, Subha
Gnana Kumar, Georgepeter
Periasamy, Vengadesh
author_facet Talebi, Sara
Daraghma, Souhad M. A.
Subramaniam, Ramesh T.
Bhassu, Subha
Gnana Kumar, Georgepeter
Periasamy, Vengadesh
author_sort Talebi, Sara
collection PubMed
description [Image: see text] Proteins have been increasingly suggested as suitable candidates for the fabrication of biological computers and other biomolecular-based electronic devices mainly due to their interesting structure-related intrinsic electrical properties. These natural biopolymers are environmentally friendly substitutes for conventional inorganic materials and find numerous applications in bioelectronics. Effective manipulation of protein biomolecules allows for accurate fabrication of nanoscaled device dimensions for miniaturized electronics. The prerequisite, however, demands an interrogation of its various electronic properties prior to understanding the complex charge transfer mechanisms in protein molecules, the knowledge of which will be crucial toward development of such nanodevices. One significantly preferred method in recent times involves the utilization of solid-state sensors where interactions of proteins could be investigated upon contact with metals such as gold. Therefore, in this work, proteins (hemoglobin and collagen) were integrated within a two-electrode system, and the resulting electronic profiles were investigated. Interestingly, structure-related electronic profiles representing semiconductive-like behaviors were observed. These characteristic electronic profiles arise from the metal (Au)–semiconductor (protein) junction, clearly demonstrating the formation of a Schottky junction. Further interpretation of the electronic behavior of proteins was done by the calculation of selected solid-state parameters. For example, the turn-on voltage of hemoglobin was measured to occur at a lower turn-on voltage, indicating the possible influence of the hem group present as a cofactor in each subunit of this tetrameric protein.
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spelling pubmed-71608412020-04-17 Printed-Circuit-Board-Based Two-Electrode System for Electronic Characterization of Proteins Talebi, Sara Daraghma, Souhad M. A. Subramaniam, Ramesh T. Bhassu, Subha Gnana Kumar, Georgepeter Periasamy, Vengadesh ACS Omega [Image: see text] Proteins have been increasingly suggested as suitable candidates for the fabrication of biological computers and other biomolecular-based electronic devices mainly due to their interesting structure-related intrinsic electrical properties. These natural biopolymers are environmentally friendly substitutes for conventional inorganic materials and find numerous applications in bioelectronics. Effective manipulation of protein biomolecules allows for accurate fabrication of nanoscaled device dimensions for miniaturized electronics. The prerequisite, however, demands an interrogation of its various electronic properties prior to understanding the complex charge transfer mechanisms in protein molecules, the knowledge of which will be crucial toward development of such nanodevices. One significantly preferred method in recent times involves the utilization of solid-state sensors where interactions of proteins could be investigated upon contact with metals such as gold. Therefore, in this work, proteins (hemoglobin and collagen) were integrated within a two-electrode system, and the resulting electronic profiles were investigated. Interestingly, structure-related electronic profiles representing semiconductive-like behaviors were observed. These characteristic electronic profiles arise from the metal (Au)–semiconductor (protein) junction, clearly demonstrating the formation of a Schottky junction. Further interpretation of the electronic behavior of proteins was done by the calculation of selected solid-state parameters. For example, the turn-on voltage of hemoglobin was measured to occur at a lower turn-on voltage, indicating the possible influence of the hem group present as a cofactor in each subunit of this tetrameric protein. American Chemical Society 2020-04-01 /pmc/articles/PMC7160841/ /pubmed/32309689 http://dx.doi.org/10.1021/acsomega.9b03831 Text en Copyright © 2020 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Talebi, Sara
Daraghma, Souhad M. A.
Subramaniam, Ramesh T.
Bhassu, Subha
Gnana Kumar, Georgepeter
Periasamy, Vengadesh
Printed-Circuit-Board-Based Two-Electrode System for Electronic Characterization of Proteins
title Printed-Circuit-Board-Based Two-Electrode System for Electronic Characterization of Proteins
title_full Printed-Circuit-Board-Based Two-Electrode System for Electronic Characterization of Proteins
title_fullStr Printed-Circuit-Board-Based Two-Electrode System for Electronic Characterization of Proteins
title_full_unstemmed Printed-Circuit-Board-Based Two-Electrode System for Electronic Characterization of Proteins
title_short Printed-Circuit-Board-Based Two-Electrode System for Electronic Characterization of Proteins
title_sort printed-circuit-board-based two-electrode system for electronic characterization of proteins
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7160841/
https://www.ncbi.nlm.nih.gov/pubmed/32309689
http://dx.doi.org/10.1021/acsomega.9b03831
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