期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 113, 期 39, 页码 10785-10790出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1606779113
关键词
oligopeptide; electron transport; self-assembled monolayer; inelastic electron tunneling spectroscopy; doping
资金
- Minerva Foundation (Munich)
- Nancy and Stephen Grand Center for Sensors and Security
- Benoziyo Endowment Fund for the Advancement of Science
- J&R Center for Scientific Research
- Kimmelman Center for Biomolecular Structure and Assembly
- Adams Fellowship of the Israel Academy of Sciences and Humanities
- Israeli Ministry of Science
Charge migration for electron transfer via the polypeptide matrix of proteins is a key process in biological energy conversion and signaling systems. It is sensitive to the sequence of amino acids composing the protein and, therefore, offers a tool for chemical control of charge transport across biomaterial-based devices. We designed a series of linear oligoalanine peptides with a single tryptophan substitution that acts as a dopant, introducing an energy level closer to the electrodes' Fermi level than that of the alanine homopeptide. We investigated the solid-state electron transport (ETp) across a self-assembled monolayer of these peptides between gold contacts. The single tryptophan doping markedly increased the conductance of the peptide chain, especially when its location in the sequence is close to the electrodes. Combining inelastic tunneling spectroscopy, UV photoelectron spectroscopy, electronic structure calculations by advanced density-functional theory, and dc current-voltage analysis, the role of tryptophan in ETp is rationalized by charge tunneling across a heterogeneous energy barrier, via electronic states of alanine and tryptophan, and by relatively efficient direct coupling of tryptophan to a Au electrode. These results reveal a controlled way of modulating the electrical properties of molecular junctions by tailor-made building block peptides.
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