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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];  [6]; ORCiD logo [7]
  1. Graduate Programs of Physics, Biology, Chemistry and Biochemistry, The Graduate Center of CUNY, New York, and Department of Biochemistry, City College of New York, New York, New York 10031, United States
  2. Department of Physics, University of California Berkeley, Berkeley, California 94720, United States; Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States
  3. Department of Physics, Columbia University, New York, New York 10027, United States
  4. Department of Chemistry, Columbia University, New York, New York 10027, United States
  5. Department of Physics, University of California Berkeley, Berkeley, California 94720, United States; Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States; Kavli Energy Nanosciences Institute at Berkeley, Berkeley, California 94720, United States
  6. Graduate Programs of Physics, Biology, Chemistry and Biochemistry, The Graduate Center of CUNY, New York, and Department of Biochemistry, City College of New York, New York, New York 10031, United States; Department of Physics, City College of New York, New York, New York 10031, United States
  7. Department of Chemistry, Columbia University, New York, New York 10027, United States; Department of Applied Physics, Columbia University, New York, New York 10027, United States
Publication Date:
Research Org.:
Lawrence Berkeley National Laboratory-National Energy Research Scientific Computing Center
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Materials Sciences & Engineering Division
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
Country of Publication:
United States
Language:
English

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. Thu . "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 = {2}
}

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