Electron transport via tyrosine-doped oligo-alanine peptide junctions : role of charges and hydrogen bonding
(2022) In Physical Chemistry Chemical Physics 24(47). p.28878-28885- Abstract
A way of modulating the solid-state electron transport (ETp) properties of oligopeptide junctions is presented by charges and internal hydrogen bonding, which affect this process markedly. The ETp properties of a series of tyrosine (Tyr)-containing hexa-alanine peptides, self-assembled in monolayers and sandwiched between gold electrodes, are investigated in response to their protonation state. Inserting a Tyr residue into these peptides enhances the ETp carried via their junctions. Deprotonation of the Tyr-containing peptides causes a further increase of ETp efficiency that depends on this residue's position. Combined results of molecular dynamics simulations and spectroscopic experiments suggest that the increased conductance upon... (More)
A way of modulating the solid-state electron transport (ETp) properties of oligopeptide junctions is presented by charges and internal hydrogen bonding, which affect this process markedly. The ETp properties of a series of tyrosine (Tyr)-containing hexa-alanine peptides, self-assembled in monolayers and sandwiched between gold electrodes, are investigated in response to their protonation state. Inserting a Tyr residue into these peptides enhances the ETp carried via their junctions. Deprotonation of the Tyr-containing peptides causes a further increase of ETp efficiency that depends on this residue's position. Combined results of molecular dynamics simulations and spectroscopic experiments suggest that the increased conductance upon deprotonation is mainly a result of enhanced coupling between the charged C-terminus carboxylate group and the adjacent Au electrode. Moreover, intra-peptide hydrogen bonding of the Tyr hydroxyl to the C-terminus carboxylate reduces this coupling. Hence, the extent of such a conductance change depends on the Tyr-carboxylate distance in the peptide's sequence.
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- author
- Guo, Cunlan ; Gavrilov, Yulian LU ; Gupta, Satyajit ; Bendikov, Tatyana ; Levy, Yaakov ; Vilan, Ayelet ; Pecht, Israel ; Sheves, Mordechai and Cahen, David
- organization
- publishing date
- 2022-11
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Physical Chemistry Chemical Physics
- volume
- 24
- issue
- 47
- pages
- 8 pages
- publisher
- Royal Society of Chemistry
- external identifiers
-
- scopus:85143537909
- pmid:36441625
- ISSN
- 1463-9076
- DOI
- 10.1039/d2cp02807g
- language
- English
- LU publication?
- yes
- id
- 31fd4cb0-799f-46e4-8b75-cd6e76de46ef
- date added to LUP
- 2023-01-20 15:50:27
- date last changed
- 2024-06-28 00:51:41
@article{31fd4cb0-799f-46e4-8b75-cd6e76de46ef,
abstract = {{<p>A way of modulating the solid-state electron transport (ETp) properties of oligopeptide junctions is presented by charges and internal hydrogen bonding, which affect this process markedly. The ETp properties of a series of tyrosine (Tyr)-containing hexa-alanine peptides, self-assembled in monolayers and sandwiched between gold electrodes, are investigated in response to their protonation state. Inserting a Tyr residue into these peptides enhances the ETp carried via their junctions. Deprotonation of the Tyr-containing peptides causes a further increase of ETp efficiency that depends on this residue's position. Combined results of molecular dynamics simulations and spectroscopic experiments suggest that the increased conductance upon deprotonation is mainly a result of enhanced coupling between the charged C-terminus carboxylate group and the adjacent Au electrode. Moreover, intra-peptide hydrogen bonding of the Tyr hydroxyl to the C-terminus carboxylate reduces this coupling. Hence, the extent of such a conductance change depends on the Tyr-carboxylate distance in the peptide's sequence.</p>}},
author = {{Guo, Cunlan and Gavrilov, Yulian and Gupta, Satyajit and Bendikov, Tatyana and Levy, Yaakov and Vilan, Ayelet and Pecht, Israel and Sheves, Mordechai and Cahen, David}},
issn = {{1463-9076}},
language = {{eng}},
number = {{47}},
pages = {{28878--28885}},
publisher = {{Royal Society of Chemistry}},
series = {{Physical Chemistry Chemical Physics}},
title = {{Electron transport <i>via </i>tyrosine-doped oligo-alanine peptide junctions : role of charges and hydrogen bonding}},
url = {{http://dx.doi.org/10.1039/d2cp02807g}},
doi = {{10.1039/d2cp02807g}},
volume = {{24}},
year = {{2022}},
}