Paper Summary: Unraveling the interplay of backbone rigidity and electron rich side-chains on electron transfer in peptides: the realization of tunable molecular wires
This paper has been selected for F1000Prime, a collection of recommended top articles in biology and medicine, contributed by the F1000 Faculty. It was recommended as being of special significance in its field.
Paper summary written by John Horsley:
Electrochemical studies were reported on a series of peptides constrained into either a 310-helix or β-strand conformation, with variable numbers of electron rich alkene containing side chains. The ability of the alkene(s) to facilitate electron transfer through the peptides by acting as a “stepping stone” was demonstrated. Furthermore, experimental data gleaned from the saturated and unsaturated tethered peptides revealed an interplay between backbone rigidity and effects arising from the alkene side-chains on electron transfer, which was also supported by theoretical studies. 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.
Authors: Horsley, JR, Yu, J, Moore, KE, Shapter, JG, Abell, AD
Work in collaboration with Flinders University