Without Contact Resistance, Proteins in Thin‐Film Solid‐State Junctions Can Be Efficient Electronic Conducting Materials

The solid-state protein junctions have shown efficient electron transport over a few tens of nanometer lengthscale. This work demonstrates, how the contact resistance ( <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"> <mml:semantics> <mml:mover><mml:msub><mml:mi>R</mml:mi> <mml:mi>C</mml:mi></mml:msub> <mml:mo>̂</mml:mo></mml:mover> <mml:annotation>$\widehat {{R_{\mathrm{C}}}}$</mml:annotation></mml:semantics> </mml:math> ) of a solid-state protein junctions, treated as a contact-limited process, which can be extracted quantitatively from the measured junction resistance (R<sub>P</sub>) by using the extrapolated zero-length resistance and series resistance (R<sub>S</sub>). Alternating current (impedance spectroscopy) and direct current measurements are used to examine charge transport in junctions of human serum albumin (HSA) and bacteriorhodopsin (bR) films with varying thicknesses. Three contact configurations, Si-Au, Au-eutectic gallium indium (EGaIn), and, in a micropore device (MpD), Au-Pd, are compared. While Si-Au and Au-EGaIn junctions exhibit substantial <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"> <mml:semantics> <mml:mover><mml:msub><mml:mi>R</mml:mi> <mml:mi>C</mml:mi></mml:msub> <mml:mo>̂</mml:mo></mml:mover> <mml:annotation>$\widehat {{R_{\mathrm{C}}}}$</mml:annotation></mml:semantics> </mml:math> that are ascribed to interfacial oxides and electrostatic protein-electrode interactions, MpD effectively eliminates <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"> <mml:semantics> <mml:mover><mml:msub><mml:mi>R</mml:mi> <mml:mi>C</mml:mi></mml:msub> <mml:mo>̂</mml:mo></mml:mover> <mml:annotation>$\widehat {{R_{\mathrm{C}}}}$</mml:annotation></mml:semantics> </mml:math> , enabling measuring the intrinsic electron transport across HSA and bR films. The exponential length-dependence of R<sub>P</sub> shows a transport decay constant (β) that varies with interfacial conditions, underscoring the role of contact engineering. By minimizing <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"> <mml:semantics> <mml:mover><mml:msub><mml:mi>R</mml:mi> <mml:mi>C</mml:mi></mml:msub> <mml:mo>̂</mml:mo></mml:mover> <mml:annotation>$\widehat {{R_{\mathrm{C}}}}$</mml:annotation></mml:semantics> </mml:math> , exceptionally low β values (≈0.7-1.1 nm<sup>-1</sup>) are found, proving that, indeed, proteins can have outstanding charge transport efficiencies.

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Publication Details

Journal
Advanced Materials
Published
2025-09-19
DOI
https://doi.org/10.1002/adma.202507654
Citations
3
Primary Topic
Photoreceptor and optogenetics research
Type
article
Field-Weighted Citation Impact
2.73
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article

Without Contact Resistance, Proteins in Thin‐Film Solid‐State Junctions Can Be Efficient Electronic Conducting Materials

Israel Pecht, David Cahen, Mordechai Sheves, Sudipta Bera et al.
3 citations
Advanced Materials
Photoreceptor and optogenetics research
2.73
article

Without Contact Resistance, Proteins in Thin‐Film Solid‐State Junctions Can Be Efficient Electronic Conducting Materials

Israel Pecht, David Cahen, Mordechai Sheves, Sudipta Bera, Ayelet Vilan, David Ehre, Sourav Das
article en
3 citations

Abstract

The solid-state protein junctions have shown efficient electron transport over a few tens of nanometer lengthscale. This work demonstrates, how the contact resistance ( <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"> <mml:semantics> <mml:mover><mml:msub><mml:mi>R</mml:mi> <mml:mi>C</mml:mi></mml:msub> <mml:mo>̂</mml:mo></mml:mover> <mml:annotation>$\widehat {{R_{\mathrm{C}}}}$</mml:annotation></mml:semantics> </mml:math> ) of a solid-state protein junctions, treated as a contact-limited process, which can be extracted quantitatively from the measured junction resistance (R<sub>P</sub>) by using the extrapolated zero-length resistance and series resistance (R<sub>S</sub>). Alternating current (impedance spectroscopy) and direct current measurements are used to examine charge transport in junctions of human serum albumin (HSA) and bacteriorhodopsin (bR) films with varying thicknesses. Three contact configurations, Si-Au, Au-eutectic gallium indium (EGaIn), and, in a micropore device (MpD), Au-Pd, are compared. While Si-Au and Au-EGaIn junctions exhibit substantial <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"> <mml:semantics> <mml:mover><mml:msub><mml:mi>R</mml:mi> <mml:mi>C</mml:mi></mml:msub> <mml:mo>̂</mml:mo></mml:mover> <mml:annotation>$\widehat {{R_{\mathrm{C}}}}$</mml:annotation></mml:semantics> </mml:math> that are ascribed to interfacial oxides and electrostatic protein-electrode interactions, MpD effectively eliminates <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"> <mml:semantics> <mml:mover><mml:msub><mml:mi>R</mml:mi> <mml:mi>C</mml:mi></mml:msub> <mml:mo>̂</mml:mo></mml:mover> <mml:annotation>$\widehat {{R_{\mathrm{C}}}}$</mml:annotation></mml:semantics> </mml:math> , enabling measuring the intrinsic electron transport across HSA and bR films. The exponential length-dependence of R<sub>P</sub> shows a transport decay constant (β) that varies with interfacial conditions, underscoring the role of contact engineering. By minimizing <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"> <mml:semantics> <mml:mover><mml:msub><mml:mi>R</mml:mi> <mml:mi>C</mml:mi></mml:msub> <mml:mo>̂</mml:mo></mml:mover> <mml:annotation>$\widehat {{R_{\mathrm{C}}}}$</mml:annotation></mml:semantics> </mml:math> , exceptionally low β values (≈0.7-1.1 nm<sup>-1</sup>) are found, proving that, indeed, proteins can have outstanding charge transport efficiencies.

Advanced MaterialsVol. 38(2)
Weizmann Institute of Science (IL)
Openalex Percentile: Top 9%
Photoreceptor and optogenetics research
2.73
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