Electron transport via tyrosine-doped oligo-alanine peptide junctions: role of charges and hydrogen bonding

Cunlan Guo, Yulian Gavrilov, Satyajit Gupta, Tatyana Bendikov, Yaakov Levy, Ayelet Vilan, Israel Pecht, Mordechai Sheves, David Cahen

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


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.

Original languageEnglish
Pages (from-to)28878-28885
Number of pages8
JournalPhysical Chemistry Chemical Physics
Issue number47
StatePublished - 7 Dec 2022
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2022 The Royal Society of Chemistry.


C. G. thanks the NSFC (21974102 and 21705019) for financial support, and the Weizmann Institute for a senior P. D. fellowship. D. C. and M. S. thank the Israel Science Foundation for financial support. M. S. thanks the Kimmelman Center for Biomolecular Structure and Assembly for partial support. The research is made possible in part by the historic generosity of the Harold Perlman family. M. S. holds the Katzir-Makineni Chair in Chemistry.

FundersFunder number
Weizmann Institute
National Natural Science Foundation of China21974102, 21705019
Israel Science Foundation


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