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Title: Probing Charge Transport through Peptide Bonds

Abstract

We measure the conductance of unmodified peptides at the single-molecule level using the scanning tunneling microscope-based break-junction method, utilizing the N-terminal amine group and the C-terminal carboxyl group as gold metal-binding linkers. Our conductance measurements of oligoglycine and oligoalanine backbones do not rely on peptide side-chain linkers. We compare our results with alkanes terminated asymmetrically with an amine group on one end and a carboxyl group on the other to show that peptide bonds decrease the conductance of an otherwise saturated carbon chain. Using a newly developed first-principles approach, we attribute the decrease in conductance to charge localization at the peptide bond, which reduces the energy of the frontier orbitals relative to the Fermi energy and the electronic coupling to the leads, lowering the tunneling probability. Crucially, this manifests as an increase in conductance decay of peptide backbones with increasing length when compared with alkanes.

Authors:
 [1]; ORCiD logo [2]; ORCiD logo [2];  [3];  [4];  [5];  [1]; ORCiD logo [6]
  1. City Univ. of New York (CUNY), NY (United States). Dept. of Biochemistry
  2. Univ. of California, Berkeley, CA (United States). Dept. of Physics; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  3. Columbia Univ., New York, NY (United States). Dept. of Physics
  4. Columbia Univ., New York, NY (United States). Dept. of Chemistry
  5. Univ. of California, Berkeley, CA (United States). Dept. of Physics; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Kavli Energy Nanosciences Inst. at Berkeley, Berkeley, CA (United States)
  6. Columbia Univ., New York, NY (United States). Dept. of Chemistry, and Dept. of Applied Physics
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). National Energy Research Scientific Computing Center (NERSC)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1484258
Grant/Contract Number:  
AC02−05CH11231
Resource Type:
Accepted Manuscript
Journal Name:
Journal of Physical Chemistry Letters
Additional Journal Information:
Journal Volume: 9; Journal Issue: 4; Journal ID: ISSN 1948-7185
Publisher:
American Chemical Society
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Brisendine, Joseph M., Refaely-Abramson, Sivan, Liu, Zhen-Fei, Cui, Jing, Ng, Fay, Neaton, Jeffrey B., Koder, Ronald L., and Venkataraman, Latha. Probing Charge Transport through Peptide Bonds. United States: N. p., 2018. Web. doi:10.1021/acs.jpclett.8b00176.
Brisendine, Joseph M., Refaely-Abramson, Sivan, Liu, Zhen-Fei, Cui, Jing, Ng, Fay, Neaton, Jeffrey B., Koder, Ronald L., & Venkataraman, Latha. Probing Charge Transport through Peptide Bonds. United States. doi:10.1021/acs.jpclett.8b00176.
Brisendine, Joseph M., Refaely-Abramson, Sivan, Liu, Zhen-Fei, Cui, Jing, Ng, Fay, Neaton, Jeffrey B., Koder, Ronald L., and Venkataraman, Latha. Sat . "Probing Charge Transport through Peptide Bonds". United States. doi:10.1021/acs.jpclett.8b00176. https://www.osti.gov/servlets/purl/1484258.
@article{osti_1484258,
title = {Probing Charge Transport through Peptide Bonds},
author = {Brisendine, Joseph M. and Refaely-Abramson, Sivan and Liu, Zhen-Fei and Cui, Jing and Ng, Fay and Neaton, Jeffrey B. and Koder, Ronald L. and Venkataraman, Latha},
abstractNote = {We measure the conductance of unmodified peptides at the single-molecule level using the scanning tunneling microscope-based break-junction method, utilizing the N-terminal amine group and the C-terminal carboxyl group as gold metal-binding linkers. Our conductance measurements of oligoglycine and oligoalanine backbones do not rely on peptide side-chain linkers. We compare our results with alkanes terminated asymmetrically with an amine group on one end and a carboxyl group on the other to show that peptide bonds decrease the conductance of an otherwise saturated carbon chain. Using a newly developed first-principles approach, we attribute the decrease in conductance to charge localization at the peptide bond, which reduces the energy of the frontier orbitals relative to the Fermi energy and the electronic coupling to the leads, lowering the tunneling probability. Crucially, this manifests as an increase in conductance decay of peptide backbones with increasing length when compared with alkanes.},
doi = {10.1021/acs.jpclett.8b00176},
journal = {Journal of Physical Chemistry Letters},
number = 4,
volume = 9,
place = {United States},
year = {2018},
month = {1}
}

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Cited by: 11 works
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Works referencing / citing this record:

Single-molecule quantum-transport phenomena in break junctions
journal, May 2019

  • Gehring, Pascal; Thijssen, Jos M.; van der Zant, Herre S. J.
  • Nature Reviews Physics, Vol. 1, Issue 6
  • DOI: 10.1038/s42254-019-0055-1

Thermoelectric properties of oligoglycine molecular wires
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  • Hou, Songjun; Wu, Qingqing; Sadeghi, Hatef
  • Nanoscale, Vol. 11, Issue 8
  • DOI: 10.1039/c8nr08878k

Charge transport through a water-assisted hydrogen bond in single-molecule glutathione disulfide junctions
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  • Yang, Wei-Yu; Zheng, Jueting; Zhang, Xia-Guang
  • Journal of Materials Chemistry C, Vol. 8, Issue 2
  • DOI: 10.1039/c9tc05686f

Doping hepta-alanine with tryptophan: A theoretical study of its effect on the electrical conductance of peptide-based single-molecule junctions
journal, May 2019

  • Schosser, Werner M.; Zotti, Linda A.; Cuevas, Juan Carlos
  • The Journal of Chemical Physics, Vol. 150, Issue 17
  • DOI: 10.1063/1.5090457