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Backbone-Constrained Peptides: Temperature and Secondary Structure Affect Solid-State Electron Transport
journal contribution
posted on 2019-12-12, 17:35 authored by Cunlan Guo, Jingxian Yu, John R. Horsley, Mordechai Sheves, David Cahen, Andrew D. AbellThe primary sequence and secondary structure of a peptide
are crucial
to charge migration, not only in solution (electron transfer, ET),
but also in the solid-state (electron transport, ETp). Hence, understanding
the charge migration mechanisms is fundamental to the development
of biomolecular devices and sensors. We report studies on four Aib-containing
helical peptide analogues: two acyclic linear peptides with one and
two electron-rich alkene-based side chains, respectively, and two
peptides that are further rigidified into a macrocycle by a side bridge
constraint, containing one or no alkene. ETp was investigated across
Au/peptide/Au junctions, between 80 and 340 K in combination with
the molecular dynamic (MD) simulations. The results reveal that the
helical structure of the peptide and electron-rich side chain both
facilitate the ETp. As temperature increases, the loss of helical
structure, change of monolayer tilt angle, and increase of thermally
activated fluctuations affect the conductance of peptides. Specifically,
room temperature conductance across the peptide monolayers correlates
well with previously observed ET rate constants, where an interplay
between backbone rigidity and electron-rich side chains was revealed.
Our findings provide new means to manipulate electronic transport
across solid-state peptide junctions.
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Aib-containing helical peptide analoguesSolid-State Electron Transportside bridge constraintelectron-rich side chainselectron-rich alkene-based side chainsET rate constantsMDETphelical structureelectron-rich side chainmonolayer tilt angleroom temperature conductancepeptide monolayers correlatescharge migration mechanisms
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