Molecular direction dependence of single-molecule conductance of a helical peptide in molecular junction

Uji, Hirotaka; Morita, Tomoyuki; Kimura, Shunsaku

doi:10.1039/c2cp43499g

Cited by 34 publications

(38 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…). Consistent with the previous results for helical peptides, summation of the local dipoles originated from electrophilic oxygens and nucleophilic nitrogens of the peptide backbone produces strong dipoles (between 90 and 120 Debye) along the helical part of each fragment (Fig. S1, Supporting Information).…”

Section: Introductionsupporting

confidence: 90%

“…This decline is consistent with the orientation of dipole moment of the peptide (Fig. S1, Supporting Information) and might be due to peptide backbone polarity . On the other hand, in fragments 2 and 3, in addition to a similar decline, the calculations indicate substantial drops in potential in several areas in the middle of the fragments (Fig.…”

Section: Introductionsupporting

confidence: 84%

See 1 more Smart Citation

On the electron transfer through Geobacter sulfurreducens PilA protein

Lebedev

Mahmud

Griva

et al. 2015

J. Polym. Sci. Part B: Polym. Phys.

View full text Add to dashboard Cite

Geobacter sulfurreducens pili composed of the Type IV pili structural peptide PilA have been implicated as efficient electronic conductors. Though investigated experimentally, no detailed theoretical studies have been performed to date that provide quantitative estimation of the transmission spectrum, electron transfer (ET) paths, efficiency of current generation, and other factors needed for understanding possible mechanisms of conductivity. In the present work, we calculate from first principles the possibilities of electron tunneling through 3 PilA fragments which structure was identified recently by NMR. The results indicate that positively charged amino acids, arginines and lysines form electrostatic traps in the middle of the peptide preventing ET at low bias voltages (<∼6 V). At higher biases the traps are filled with electrons making possible sequential electron tunneling through the central part of the protein. In addition, leucines and phenylalanines form ET loops facilitating electron stabilization within the protein and sequential ET. Our results indicate that ET through the PilA protein cannot occur by coherent ET, but suggest a sequential (incoherent) mechanism. © 2015 Wiley Periodicals, Inc. J. Polym. Sci., Part B: Polym. Phys. 2015, 53, 1706–1717

show abstract

Section: Introductionsupporting

confidence: 90%

Section: Introductionsupporting

confidence: 84%

On the electron transfer through Geobacter sulfurreducens PilA protein

Lebedev

Mahmud

Griva

et al. 2015

J. Polym. Sci. Part B: Polym. Phys.

View full text Add to dashboard Cite

show abstract

“…Recently, Uji and coworkers have reported helical 8mer peptides with an alternating sequence of Ala‐Aib, designed for specific adsorption onto the gold surface 118. The peptide was immobilized in two opposite directions of the helix dipole with respect to the gold surface.…”

Section: Nanoscale Molecular Junctionsmentioning

confidence: 99%

Electron Transport Mediated by Peptides Immobilized on Surfaces

Juhaniewicz

Pawłowski

Sęk

2015

Israel Journal of Chemistry

View full text Add to dashboard Cite

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.

show abstract

“…Conceivably, E ex is one of the important elements that should not be ignored in the charge transfer process. However, although there are some studies on peptides in E ex , they mostly report that whether the peptides are suitable as the peptides‐based electronic devices or which kind of electronic devices the peptides are suitable for . For instance, alpha‐helix peptides show different currents under the E ex in antiparallel and parallel with the intrinsic dipole moment of the peptides, and thus they are suitable for the design of peptide semiconductors .…”

Section: Introductionmentioning

confidence: 99%

“…However, although there are some studies on peptides in E ex , they mostly report that whether the peptides are suitable as the peptides-based electronic devices or which kind of electronic devices the peptides are suitable for. [62][63][64][65][66][67][68][69][70][71] For instance, alpha-helix peptides show different currents under the E ex in antiparallel and parallel with the intrinsic dipole moment of the peptides, and thus they are suitable for the design of peptide semiconductors. [72] However, there are not detailed or systematic descriptions about how the E ex with different directions and strengths influence the ET behavior of peptides and their corresponding electronic properties.…”

Section: Introductionmentioning

confidence: 99%

Nonlinear Migration Dynamics of Excess Electrons along Linear Oligopeptides Controlled by an Applied Electric Field

Song

2019

ChemPhysChem

View full text Add to dashboard Cite

Migration of an excess electron along linear oligopeptides governed by the external electric field (Eex) which is against the inner dipole electric field is theoretically investigated, including the effects of Eex on the structural and electronic properties of electron migration. Two structural properties including electron‐binding ability and the dipole moment of linear oligopeptides are sensitive to the Eex values and can be largely modulated by Eex due to the competition of Eex and the inner electric field and electron transfer caused by Eex. In the case of low Eex values, two structural properties decrease slightly, while for high Eex values, the electron‐binding ability continually increases strongly, with dipole moments firstly increasing significantly and then increasing more slowly at higher Eex. Additionally, linear oligopeptides of different chain lengths influence the modulation extent of Eex and the longer the chain length is, the more sensitive modulation of Eex is. In addition, electronic properties represented by electron spin densities and singly occupied molecular orbital distributions vary with Eex intensities, leading to an unusual electron migration behavior. As Eex increases, an excess electron transfers from the N‐terminus to the C‐terminus and jumps over a neighboring dipole unit of two termini to other units, respectively, instead of transferring by means of a one‐by‐one dipole unit hopping mechanism. These findings not only promote a deeper understanding of the connection between Eex and structural and electronic properties of electron transfer behavior in peptides, but also provide a new insight into the modulation of electron migration along the oligopeptides.

show abstract

Molecular direction dependence of single-molecule conductance of a helical peptide in molecular junction

Cited by 34 publications

References 26 publications

On the electron transfer through Geobacter sulfurreducens PilA protein

On the electron transfer through Geobacter sulfurreducens PilA protein

Electron Transport Mediated by Peptides Immobilized on Surfaces

Nonlinear Migration Dynamics of Excess Electrons along Linear Oligopeptides Controlled by an Applied Electric Field

Contact Info

Product

Resources

About