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Issue 29, 2012
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Intermolecular interactions in electron transfer through stretched helical peptides

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Abstract

The helical peptide Cys-Ala-Lys-(Glu-Ala-Ala-Ala-Lys)2-Ala-NH-(CH2)2-SH has been organized forming a self-assembled monolayer on gold (0.602 peptides per nm2), its conductance behavior under stretching conditions being studied using scanning tunnelling microscopy and current sensing atomic force microscopy. The helical conformation of the peptide has been found to play a fundamental role in the conductance. Moreover, variation of the current upon molecular stretching indicates that peptides can be significantly elongated before the conductance drops to zero, the critical elongation being 1.22 ± 0.47 nm. Molecular dynamics simulations of a single peptide in the free state and of a variable number of peptides tethered to a gold surface (i.e. densities ranging from 0.026 to 1.295 peptides per nm2) have indicated that the helical conformation is intrinsically favored in solvated environments while in desolvated environments it is retained because of the fundamental role played by peptidepeptide intermolecular interactions. The structure obtained for the system with 24 tethered peptides, with a density of 0.634 peptides per nm2 closest to the experimental one, is in excellent agreement with experimental observations. On the other hand, simulations in which a single molecule is submitted to different compression and stretching processes while the rest remain in the equilibrium have been used to mimic the variation of the tip–substrate distance in experimental measures. Results allowed us to identify the existence, and in some cases coexistence, of intermolecular and intramolecular ionic ladders, suggesting that peptide-mediated electron transfer occurs through the hopping mechanism. Finally, quantum mechanical calculations have been used to investigate the variation of the electronic structure upon compression and stretching deformations.

Graphical abstract: Intermolecular interactions in electron transfer through stretched helical peptides

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Publication details

The article was received on 09 Mar 2012, accepted on 21 May 2012 and first published on 27 Jun 2012


Article type: Paper
DOI: 10.1039/C2CP40761B
Citation: Phys. Chem. Chem. Phys., 2012,14, 10332-10344
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    Intermolecular interactions in electron transfer through stretched helical peptides

    D. E. López-Pérez, G. Revilla-López, D. Jacquemin, D. Zanuy, B. Palys, S. Sek and C. Alemán, Phys. Chem. Chem. Phys., 2012, 14, 10332
    DOI: 10.1039/C2CP40761B

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