Review peptides and proteins wired into the electrical circuits: An SPM‐based approach

Sęk, Sławomir

doi:10.1002/bip.22148

Cited by 39 publications

(32 citation statements)

References 62 publications

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“…Peptide molecular junctions have considerable potential to serve as functional devices. Most of them are supposed to take advantage of the complex electron transport behavior of the peptides 109. This includes the directional dependence of electron transport and the modulation of the conductance induced by structural changes.…”

Section: Nanoscale Molecular Junctionsmentioning

confidence: 99%

Electron Transport Mediated by Peptides Immobilized on Surfaces

Juhaniewicz

Pawłowski

Sęk

2015

Israel Journal of Chemistry

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The tetragonal compound FeF3(H2O)3 is synthesized through a facile liquid‐phase method. FeF3(H2O)3/C is prepared by mechanical milling with carbon black and investigated for its application as a cathode material. This material exhibits two types of thermodynamic lithiation scheme, at 3.0 and 1.5 V, which correspond to a Li+‐intercalation process (1 Li+) and a conversion reaction (>1 Li+), respectively. A reversible capacity of about 300 mAh g−1 can be achieved at a current density of 10 mAg−1. In particular, the intercalation/deintercalation process above 2.0 V exhibits good cycling performance and rate properties. The relatively high diffusion coefficients (Dcv=7.27×10−13–1.07×10−12 m2 s−1) of Li+ through the FeF3(H2O)3 lattice are calculated by using the Randles–Sevcik equation, which reveal fast Li+‐ion migration in this process. In contrast, the conversion reaction is strongly dependent on the current density. Electrochemical impedance spectroscopy indicates that the FeF3(H2O)3/C cathode forms a relatively stable solid electrolyte interphase film, with a low Schottky contact resistance in comparison with that of the FeF3/C cathode, which makes it a potential candidate for cathode applications.

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Section: Nanoscale Molecular Junctionsmentioning

confidence: 99%

Electron Transport Mediated by Peptides Immobilized on Surfaces

Juhaniewicz

Pawłowski

Sęk

2015

Israel Journal of Chemistry

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“…[1] Peptides present as ideal candidates for such ap urpose. In particular,p eptides can self-assemble on ac onducting surface such as gold [2] or silicon, [3] while also having an ability to be specifically functionalized along their backbonet oe nablep recision-branching, ac ritical factor in the design of well-definedt hree-dimensional molecular circuitry. [4] Peptides are readily synthesized to ap redisposeds ize and geometry,p articularly the secondary structure, [5] which is known to influence the efficiency of electron transfer.…”

Section: Introductionmentioning

confidence: 99%

The Correlation of Electrochemical Measurements and Molecular Junction Conductance Simulations in β‐Strand Peptides

Horsley

2015

Chemistry A European J

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Understanding the electronic properties of single peptides is not only of fundamental importance, but it is also paramount to the realization of peptide-based molecular electronic components. Electrochemical and theoretical studies are reported on two β-strand-based peptides, one with its backbone constrained with a triazole-containing tether introduced by Huisgen cycloaddition (peptide 1) and the other a direct linear analogue (peptide 2). Density functional theory (DFT) and non-equilibrium Green's function were used to investigate conductance in molecular junctions containing peptides 3 and 4 (analogues of 1 and 2). Although the peptides share a common β-strand conformation, they display vastly different electronic transport properties due to the presence (or absence) of the side-bridge constraint and the associated effect on backbone rigidity. These studies reveal that the electron transfer rate constants of 1 and 2, and the conductance calculated for 3 and 4, differ by approximately one order of magnitude, thus providing two distinctly different conductance states and what is essentially a molecular switch. A definitive correlation of electrochemical measurements and molecular junction conductance simulations is demonstrated using two different charge transfer techniques. This study furthers our understanding of the electronic properties of peptides at the molecular level, which provides an opportunity to fine-tune their molecular orbital energies through suitable structural manipulation.

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“…oligopeptide | electron transport | self-assembled monolayer | inelastic electron tunneling spectroscopy | doping E lectron transfer (ET) processes taking place between prosthetic groups across the polypeptide matrices of proteins (1-3) have been extensively explored by, e.g., time-resolved photolysis (4,5), pulse radiolysis (6, 7), scanning tunneling microscopy (8,9), electrochemical methods (10)(11)(12), and by theoretical studies (13)(14)(15)(16). The surprisingly fast and efficient ET over considerable distances (up to ∼25 Å) (17) via peptide matrices in proteins suggests possible development of peptide-and protein-based bioelectronics with diverse functionality and relative ease of modification (18,19).…”

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Tuning electronic transport via hepta-alanine peptides junction by tryptophan doping

Guo

Refaely-Abramson

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

111

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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 selfassembled 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 tailormade "building block" peptides. oligopeptide | electron transport | self-assembled monolayer | inelastic electron tunneling spectroscopy | doping E lectron transfer (ET) processes taking place between prosthetic groups across the polypeptide matrices of proteins (1-3) have been extensively explored by, e.g., time-resolved photolysis (4, 5), pulse radiolysis (6, 7), scanning tunneling microscopy (8, 9), electrochemical methods (10-12), and by theoretical studies (13-16). The surprisingly fast and efficient ET over considerable distances (up to ∼25 Å) (17) via peptide matrices in proteins suggests possible development of peptide-and protein-based bioelectronics with diverse functionality and relative ease of modification (18,19). Studying electron transport (ETp) via solid-state molecular junctions represents an approach, bridging the study of basic ET-related phenomena and electronic devices, where measuring ET rates as a function of an electrochemical driving force is replaced by measuring current across molecular junctions as a function of an applied electrical voltage (20). Combining the concepts and methods of molecular electronics such as currentvoltage (I-V) line-shape analysis (21, 22), temperature-dependent measurements (23, 24), and electronic spectroscopy techniques (25-27) may yield new insights into the mechanism of ETp across the peptide matrix of proteins (28-30) and pave the road to peptide-and protein-based electronic devices for switching, rectification, and memory (18, 31).ETp via homopeptides has been investigated, probing the roles of specific amino acid residues, their protonation, and secondary structure (29,32). Synthetic heteropeptides with defined compositi...

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Review peptides and proteins wired into the electrical circuits: An SPM‐based approach

Cited by 39 publications

References 62 publications

Electron Transport Mediated by Peptides Immobilized on Surfaces

Electron Transport Mediated by Peptides Immobilized on Surfaces

The Correlation of Electrochemical Measurements and Molecular Junction Conductance Simulations in β‐Strand Peptides

Tuning electronic transport via hepta-alanine peptides junction by tryptophan doping

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