Self-assembly of peptides provides the possibility of achieving relatively long range order on surfaces. These ordered peptides can also form channels that can be used as conduction channels. In the past, studies were focused on electron conduction through the secondary structure and amine bond of peptides and these restrict conduction of electrons over a short range (a few nanometers). In this work, we demonstrate the realization of electron conduction over a longer range of a few hundred nanometers via π-π stacking of the phenyl groups in the tyrosine residue of a single peptide. The peptide used in this work was designed with a phenyl ring for π-π stacking at one end and a carboxylic group at the other end for binding to aminopropyltriethoxysilane (APTES) treated silicon wafer. The distance between the peptides is controlled by a disulfide bond formed between neighboring cysteine residue and also by the amine groups of aminopropyltriethoxysilane. We demonstrate that the self-assembled peptide is conducting in the dry state over hundreds of nanometers, realizing the possibility of using peptide as a molecular wire.
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