Solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling

Successful integration of proteins in solid-state electronics requires contacting them in a non-invasive fashion, with a solid conducting surface for immobilization as one such contact. The contacts can affect and even dominate the measured electronic transport. Often substrates, substrate treatment...

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Main Authors: Mukhopadhyay, Sabyasachi, Karuppannan, Senthil Kumar, Guo, Cunlan, Fereiro, Jerry A., Bergren, Adam, Mukundan, Vineetha, Qiu, Xinkai, Castañeda Ocampo, Olga E., Chen, Xiaoping, Chiechi, Ryan C., McCreery, Richard, Pecht, Israel, Sheves, Mordechai, Pasula, Rupali Reddy, Lim, Sierin, Nijhuis, Christian A., Vilan, Ayelet, Cahen, David
Other Authors: School of Chemical and Biomedical Engineering
Format: Article
Language:English
Published: 2020
Subjects:
Online Access:https://hdl.handle.net/10356/145612
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Institution: Nanyang Technological University
Language: English
id sg-ntu-dr.10356-145612
record_format dspace
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Engineering::Chemical engineering
Solid-state
Electronic Coupling
spellingShingle Engineering::Chemical engineering
Solid-state
Electronic Coupling
Mukhopadhyay, Sabyasachi
Karuppannan, Senthil Kumar
Guo, Cunlan
Fereiro, Jerry A.
Bergren, Adam
Mukundan, Vineetha
Qiu, Xinkai
Castañeda Ocampo, Olga E.
Chen, Xiaoping
Chiechi, Ryan C.
McCreery, Richard
Pecht, Israel
Sheves, Mordechai
Pasula, Rupali Reddy
Lim, Sierin
Nijhuis, Christian A.
Vilan, Ayelet
Cahen, David
Solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling
description Successful integration of proteins in solid-state electronics requires contacting them in a non-invasive fashion, with a solid conducting surface for immobilization as one such contact. The contacts can affect and even dominate the measured electronic transport. Often substrates, substrate treatments, protein immobilization, and device geometries differ between laboratories. Thus the question arises how far results from different laboratories and platforms are comparable and how to distinguish genuine protein electronic transport properties from platform-induced ones. We report a systematic comparison of electronic transport measurements between different laboratories, using all commonly used large-area schemes to contact a set of three proteins of largely different types. Altogether we study eight different combinations of molecular junction configurations, designed so that Ageoof junctions varies from 105 to 10-3 μm2. Although for the same protein, measured with similar device geometry, results compare reasonably well, there are significant differences in current densities (an intensive variable) between different device geometries. Likely, these originate in the critical contact-protein coupling (∼contact resistance), in addition to the actual number of proteins involved, because the effective junction contact area depends on the nanometric roughness of the electrodes and at times, even the proteins may increase this roughness. On the positive side, our results show that understanding what controls the coupling can make the coupling a design knob. In terms of extensive variables, such as temperature, our comparison unanimously shows the transport to be independent of temperature for all studied configurations and proteins. Our study places coupling and lack of temperature activation as key aspects to be considered in both modeling and practice of protein electronic transport experiments.
author2 School of Chemical and Biomedical Engineering
author_facet School of Chemical and Biomedical Engineering
Mukhopadhyay, Sabyasachi
Karuppannan, Senthil Kumar
Guo, Cunlan
Fereiro, Jerry A.
Bergren, Adam
Mukundan, Vineetha
Qiu, Xinkai
Castañeda Ocampo, Olga E.
Chen, Xiaoping
Chiechi, Ryan C.
McCreery, Richard
Pecht, Israel
Sheves, Mordechai
Pasula, Rupali Reddy
Lim, Sierin
Nijhuis, Christian A.
Vilan, Ayelet
Cahen, David
format Article
author Mukhopadhyay, Sabyasachi
Karuppannan, Senthil Kumar
Guo, Cunlan
Fereiro, Jerry A.
Bergren, Adam
Mukundan, Vineetha
Qiu, Xinkai
Castañeda Ocampo, Olga E.
Chen, Xiaoping
Chiechi, Ryan C.
McCreery, Richard
Pecht, Israel
Sheves, Mordechai
Pasula, Rupali Reddy
Lim, Sierin
Nijhuis, Christian A.
Vilan, Ayelet
Cahen, David
author_sort Mukhopadhyay, Sabyasachi
title Solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling
title_short Solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling
title_full Solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling
title_fullStr Solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling
title_full_unstemmed Solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling
title_sort solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling
publishDate 2020
url https://hdl.handle.net/10356/145612
_version_ 1787136502478667776
spelling sg-ntu-dr.10356-1456122023-12-29T06:47:05Z Solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling Mukhopadhyay, Sabyasachi Karuppannan, Senthil Kumar Guo, Cunlan Fereiro, Jerry A. Bergren, Adam Mukundan, Vineetha Qiu, Xinkai Castañeda Ocampo, Olga E. Chen, Xiaoping Chiechi, Ryan C. McCreery, Richard Pecht, Israel Sheves, Mordechai Pasula, Rupali Reddy Lim, Sierin Nijhuis, Christian A. Vilan, Ayelet Cahen, David School of Chemical and Biomedical Engineering Engineering::Chemical engineering Solid-state Electronic Coupling Successful integration of proteins in solid-state electronics requires contacting them in a non-invasive fashion, with a solid conducting surface for immobilization as one such contact. The contacts can affect and even dominate the measured electronic transport. Often substrates, substrate treatments, protein immobilization, and device geometries differ between laboratories. Thus the question arises how far results from different laboratories and platforms are comparable and how to distinguish genuine protein electronic transport properties from platform-induced ones. We report a systematic comparison of electronic transport measurements between different laboratories, using all commonly used large-area schemes to contact a set of three proteins of largely different types. Altogether we study eight different combinations of molecular junction configurations, designed so that Ageoof junctions varies from 105 to 10-3 μm2. Although for the same protein, measured with similar device geometry, results compare reasonably well, there are significant differences in current densities (an intensive variable) between different device geometries. Likely, these originate in the critical contact-protein coupling (∼contact resistance), in addition to the actual number of proteins involved, because the effective junction contact area depends on the nanometric roughness of the electrodes and at times, even the proteins may increase this roughness. On the positive side, our results show that understanding what controls the coupling can make the coupling a design knob. In terms of extensive variables, such as temperature, our comparison unanimously shows the transport to be independent of temperature for all studied configurations and proteins. Our study places coupling and lack of temperature activation as key aspects to be considered in both modeling and practice of protein electronic transport experiments. Ministry of Education (MOE) Published version S.M. thanks SERB-DST, Govt. of India (award No. ECR/2017/001937 ) research grants, and the Council for Higher Education (Israel) for a postdoctoral research fellowship at the initial stage of this work. J.F. thanks the Azrieli Foundation for a PD fellowship; C.G. acknowledges a Dean's PD fellowship. At WIS, we thank Dr. Noga Friedman for bR samples, the Minerva Foundation (Munich) and the Israel Science Foundation for partial support. NUS research groups acknowledge the Ministry of Education (MOE) for supporting this research under award No. MOE2015-T2-2-134. Prime Minister’s Office, Singapore, under its medium-sized centre program, is also acknowledged for supporting this research. At Groningen the Zernike Institute of Advanced Materials is gratefully acknowledged for financial support. R.M. thanks the Zernike Institute of Advanced Materials; R.C. and V.M. thank the University of Alberta & Alberta Innovates, and R.C. and A.B. thank the National Research Council Canada for financial support. 2020-12-30T03:05:04Z 2020-12-30T03:05:04Z 2020 Journal Article Mukhopadhyay, S., Karuppannan, S. K., Guo, C., Fereiro, J. A., Bergren, A., Mukundan, V., . . . Cahen, D. (2020). Solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling. iScience, 23(5), 101099-. doi:10.1016/j.isci.2020.101099 2589-0042 https://hdl.handle.net/10356/145612 10.1016/j.isci.2020.101099 32438319 5 23 en MOE2015-T2-2-134 iScience © 2020 The Author(s). This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). application/pdf