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Conformation- and phosphorylation-dependent electron tunnelling across self-assembled monolayers of tau peptides

Ashkarran, Ali Akbar ; Hosseini, Atiyeh LU ; Loloee, Reza ; Perry, George ; Lee, Ki Bum ; Lund, Mikael LU orcid ; Ejtehadi, Mohammad Reza and Mahmoudi, Morteza (2022) In Journal of Colloid and Interface Science 606. p.2038-2050
Abstract

We report on charge transport across self-assembled monolayers (SAMs) of short tau peptides by probing the electron tunneling rates and quantum mechanical simulation. We measured the electron tunneling rates across SAMs of carboxyl-terminated linker molecules (C6H12O2S) and short cis-tau (CT) and trans-tau (TT) peptides, supported on template-stripped gold (AuTS) bottom electrode, with Eutectic Gallium-Indium (EGaIn)(EGaIn) top electrode. Measurements of the current density across thousands of AuTS/linker/tau//Ga2O3/EGaIn single-molecule junctions show that the tunneling current across CT peptide is one order of magnitude lower than that of TT peptide. Quantum... (More)

We report on charge transport across self-assembled monolayers (SAMs) of short tau peptides by probing the electron tunneling rates and quantum mechanical simulation. We measured the electron tunneling rates across SAMs of carboxyl-terminated linker molecules (C6H12O2S) and short cis-tau (CT) and trans-tau (TT) peptides, supported on template-stripped gold (AuTS) bottom electrode, with Eutectic Gallium-Indium (EGaIn)(EGaIn) top electrode. Measurements of the current density across thousands of AuTS/linker/tau//Ga2O3/EGaIn single-molecule junctions show that the tunneling current across CT peptide is one order of magnitude lower than that of TT peptide. Quantum mechanical simulation demonstrated a wider energy bandgap of the CT peptide, as compared to the TT peptide, which causes a reduction in its electron tunneling current. Our findings also revealed the critical role of phosphorylation in altering the charge transport characteristics of short peptides; more specifically, we found that the presence of phosphate groups can reduce the energy band gap in tau peptides and alter their electrical properties. Our results suggest that conformational and phosphorylation of short peptides (e.g., tau) can significantly change their charge transport characteristics and energy levels.

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author
; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Charge transport, Cis-tau peptide, Conformation, Phosphorylation, Quantum mechanical simulation, Trans-tau peptide
in
Journal of Colloid and Interface Science
volume
606
pages
13 pages
publisher
Elsevier
external identifiers
  • pmid:34749450
  • scopus:85117895561
ISSN
0021-9797
DOI
10.1016/j.jcis.2021.09.185
language
English
LU publication?
yes
additional info
Publisher Copyright: © 2021 Elsevier Inc.
id
b6013a5b-0d1d-45c1-ac41-ac629aefee86
date added to LUP
2021-11-12 12:06:24
date last changed
2024-12-01 14:34:43
@article{b6013a5b-0d1d-45c1-ac41-ac629aefee86,
  abstract     = {{<p>We report on charge transport across self-assembled monolayers (SAMs) of short tau peptides by probing the electron tunneling rates and quantum mechanical simulation. We measured the electron tunneling rates across SAMs of carboxyl-terminated linker molecules (C<sub>6</sub>H<sub>12</sub>O<sub>2</sub>S) and short cis-tau (CT) and trans-tau (TT) peptides, supported on template-stripped gold (Au<sup>TS</sup>) bottom electrode, with Eutectic Gallium-Indium (EGaIn)(EGaIn) top electrode. Measurements of the current density across thousands of Au<sup>TS</sup>/linker/tau//Ga<sub>2</sub>O<sub>3</sub>/EGaIn single-molecule junctions show that the tunneling current across CT peptide is one order of magnitude lower than that of TT peptide. Quantum mechanical simulation demonstrated a wider energy bandgap of the CT peptide, as compared to the TT peptide, which causes a reduction in its electron tunneling current. Our findings also revealed the critical role of phosphorylation in altering the charge transport characteristics of short peptides; more specifically, we found that the presence of phosphate groups can reduce the energy band gap in tau peptides and alter their electrical properties. Our results suggest that conformational and phosphorylation of short peptides (e.g., tau) can significantly change their charge transport characteristics and energy levels.</p>}},
  author       = {{Ashkarran, Ali Akbar and Hosseini, Atiyeh and Loloee, Reza and Perry, George and Lee, Ki Bum and Lund, Mikael and Ejtehadi, Mohammad Reza and Mahmoudi, Morteza}},
  issn         = {{0021-9797}},
  keywords     = {{Charge transport; Cis-tau peptide; Conformation; Phosphorylation; Quantum mechanical simulation; Trans-tau peptide}},
  language     = {{eng}},
  month        = {{01}},
  pages        = {{2038--2050}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Colloid and Interface Science}},
  title        = {{Conformation- and phosphorylation-dependent electron tunnelling across self-assembled monolayers of tau peptides}},
  url          = {{http://dx.doi.org/10.1016/j.jcis.2021.09.185}},
  doi          = {{10.1016/j.jcis.2021.09.185}},
  volume       = {{606}},
  year         = {{2022}},
}