Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/92374
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Type: Journal article
Title: Unraveling the interplay of backbone rigidity and electron rich side-chains on electron transfer in peptides: the realization of tunable molecular wires
Author: Horsley, J.
Yu, J.
Moore, K.
Shapter, J.
Abell, A.
Citation: Journal of the American Chemical Society, 2014; 136(35):12479-12488
Publisher: American Chemical Society
Issue Date: 2014
ISSN: 0002-7863
1520-5126
Statement of
Responsibility: 
John R. Horsley, Jingxian Yu, Katherine E. Moore, Joe G. Shapter, and Andrew D. Abell
Abstract: Electrochemical studies are reported on a series of peptides constrained into either a 310-helix (1-6) or β-strand (7-9) conformation, with variable numbers of electron rich alkene containing side chains. Peptides (1 and 2) and (7 and 8) are further constrained into these geometries with a suitable side chain tether introduced by ring closing metathesis (RCM). Peptides 1, 4 and 5, each containing a single alkene side chain reveal a direct link between backbone rigidity and electron transfer, in isolation from any effects due to the electronic properties of the electron rich side-chains. Further studies on the linear peptides 3-6 confirm the ability of the alkene to facilitate electron transfer through the peptide. A comparison of the electrochemical data for the unsaturated tethered peptides (1 and 7) and saturated tethered peptides (2 and 8) reveals an interplay between backbone rigidity and effects arising from the electron rich alkene side-chains on electron transfer. Theoretical calculations on β-strand models analogous to 7, 8 and 9 provide further insights into the relative roles of backbone rigidity and electron rich side-chains on intramolecular electron transfer. Furthermore, electron population analysis confirms the role of the alkene as a "stepping stone" for electron transfer. These findings provide a new approach for fine-tuning the electronic properties of peptides by controlling backbone rigidity, and through the inclusion of electron rich side-chains. This allows for manipulation of energy barriers and hence conductance in peptides, a crucial step in the design and fabrication of molecular-based electronic devices.
Keywords: Alkenes; Peptides; Protein Structure, Secondary; Electron Transport; Hydrogen Bonding; Electrons; Models, Molecular; Electrochemical Techniques
Rights: Copyright © 2014 American Chemical Society
RMID: 0030007765
DOI: 10.1021/ja507175b
Appears in Collections:IPAS publications

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