Cold denaturation induces inversion of dipole and spin transfer in chiral peptide monolayers

Eckshtain-Levi, Meital; Capua, Eyal; Refaely-Abramson, Sivan; Sarkar, Soumyajit; Gavrilov, Yulian; Mathew, S. P.; Paltiel, Yossi; Levy, Yaakov; Kronik, Leeor; Naaman, Ron

doi:10.1038/ncomms10744

Cited by 98 publications

(123 citation statements)

References 53 publications

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“…The spin filtering ability can be tuned by various means, for example, by varying the length of the chiral molecule, 8,9,13 by exposure to light, 22 or by varying the temperature. 23 The sign of the favored spin can be reversed by light, as was shown for an oligopeptide-CdSe hybrid 22 and also by lowering the temperature, which causes cold denaturation of the peptide-made monolayers, as seen in an oligopeptide-CdSe hybrid studied in the Hall configuration. 23 It was also found that for given oligomers (DNA or peptides) longer molecules lead to better spin filtering.…”

Section: Introductionmentioning

confidence: 86%

“…23 The sign of the favored spin can be reversed by light, as was shown for an oligopeptide-CdSe hybrid 22 and also by lowering the temperature, which causes cold denaturation of the peptide-made monolayers, as seen in an oligopeptide-CdSe hybrid studied in the Hall configuration. 23 It was also found that for given oligomers (DNA or peptides) longer molecules lead to better spin filtering. 8,9,13 Thus, there is abundant experimental evidence that the CISS effect depends on the structural parameters of the chiral molecules.…”

Section: Introductionmentioning

confidence: 86%

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Structure dependent spin selectivity in electron transport through oligopeptides

Kiran

Cohen

Naaman

2016

The Journal of Chemical Physics

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108

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The chiral-induced spin selectivity (CISS) effect entails spin-selective electron transmission through chiral molecules. In the present study, the spin filtering ability of chiral, helical oligopeptide monolayers of two different lengths is demonstrated using magnetic conductive probe atomic force microscopy. Spin-specific nanoscale electron transport studies elucidate that the spin polarization is higher for 14-mer oligopeptides than that of the 10-mer. We also show that the spin filtering ability can be tuned by changing the tip-loading force applied on the molecules. The spin selectivity decreases with increasing applied force, an effect attributed to the increased ratio of radius to pitch of the helix upon compression and increased tilt angles between the molecular axis and the surface normal. The method applied here provides new insights into the parameters controlling the CISS effect. C 2016 Author(s). All article content, except where otherwise noted, is licensed under a Creative Commons Attribution (CC BY) license

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Section: Introductionmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 86%

Structure dependent spin selectivity in electron transport through oligopeptides

Kiran

Cohen

Naaman

2016

The Journal of Chemical Physics

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108

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“…Notice that Franklike reaction networks imply that, in the chiral recognition between enantiomers, the heterochiral interaction is much stronger that the homochiral one. In this respect, most chiral organic compounds show preferential heterochiral interactions, but some show preferential homochiral interactions [33,34], which is highly significant in a biological context. As a consequence, for these latter types of compounds, Frank-like reaction networks cannot be taken into account or invoked as possible SMSB systems.…”

Section: Frank-like Reaction Networkmentioning

confidence: 99%

Spontaneous mirror symmetry breaking and origin of biological homochirality

Ribó

Hochberg

Crusats

et al. 2017

J. R. Soc. Interface.

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Recent reports on both theoretical simulations and on the physical chemistry basis of spontaneous mirror symmetry breaking (SMSB), that is, asymmetric synthesis in the absence of any chiral polarizations other than those arising from the chiral recognition between enantiomers, strongly suggest that the same nonlinear dynamics acting during the crucial stages of abiotic chemical evolution leading to the formation and selection of instructed polymers and replicators, would have led to the homochirality of instructed polymers. We review, in the first instance, which reaction networks lead to the nonlinear kinetics necessary for SMSB, and the thermodynamic features of the systems where this potentiality may be realized. This could aid not only in the understanding of SMSB, but also the design of reliable scenarios in abiotic evolution where biological homochirality could have taken place. Furthermore, when the emergence of biological chirality is assumed to occur during the stages of chemical evolution leading to the selection of polymeric species, one may hypothesize on a tandem track of the decrease of symmetry order towards biological homochirality, and the transition from the simple chemistry of astrophysical scenarios to the complexity of systems chemistry yielding Darwinian evolution.

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“…DFTbased transport calculations are very sensitive to level alignment issues (46) and more accurate theories would be prohibitively expensive here. Therefore, to assess if the presence of Trp affects the frontier molecular orbital energy levels of the whole peptide, we performed DFT calculations using an optimally tuned range-separated hybrid functional to evaluate the accurate detailed electronic structures of the peptides in the gas phase (32,(47)(48)(49). Unlike in standard DFT approximations the HOMO level from this approach corresponds to the negative of the ionization potential, −IP, a key parameter determining energy alignment for transport.…”

Section: Significancementioning

confidence: 99%

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

Guo

Refaely-Abramson

et al. 2016

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

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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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Cold denaturation induces inversion of dipole and spin transfer in chiral peptide monolayers

Cited by 98 publications

References 53 publications

Structure dependent spin selectivity in electron transport through oligopeptides

Structure dependent spin selectivity in electron transport through oligopeptides

Spontaneous mirror symmetry breaking and origin of biological homochirality

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

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