TY - JOUR
T1 - Probing Charge Transport through Peptide Bonds
AU - Brisendine, Joseph M.
AU - Refaely-Abramson, Sivan
AU - Liu, Zhen-Fei
AU - Cui, Jing
AU - Ng, Fay
AU - Neaton, Jeffrey B.
AU - Koder, Ronald L.
AU - Venkataraman, Latha
N1 - The experimental work was supported in part by the National Science Foundation (Award No. DMR-1507440). S.R.A. acknowledges Rothschild and Fulbright fellowships. R.L.K. acknowledges support via National Institutes of Health Grant 1R01-GM111932 and the program and infrastructure support from the National Institutes of Health National Center for Research Resources to the City College of New York (5G12MD007603-30). The computational part of this work was supported by the U.S. Department of Energy, Office of Basic Energy Sciences, Materials Sciences and Engineering Division, under Contract No. DE-AC02−05CH11231. A portion of this work was also supported by the Molecular Foundry through the U.S. Department of Energy, Office of Basic Energy Sciences, under the same contract number. A portion of the computation work was done using NERSC resources. J.M.B., S.R.-A., and Z.-F.L. contributed equally
PY - 2018/2/15
Y1 - 2018/2/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85042183548&partnerID=8YFLogxK
U2 - 10.1021/acs.jpclett.8b00176
DO - 10.1021/acs.jpclett.8b00176
M3 - مقالة
SN - 1948-7185
VL - 9
SP - 763
EP - 767
JO - Journal of Physical Chemistry Letters
JF - Journal of Physical Chemistry Letters
IS - 4
ER -