Histidine works as an important mediator in the charge transport process through proteins via its conjugate side group. It can also stabilize a peptide's secondary structure through hydrogen bonding of the imidazole group. In this study, the conformation of the self-assembled monolayer (SAM) and the charge transport of the tailor-made oligopeptide hepta-histidine derivative (7-His) were modulated through the pH control of the assembly environment. Histidine is found to be an efficient tunneling mediator in monolayer junctions with an attenuation factor of β = ∼0.5 Å-1. Successful theoretical model fitting indicates a linear increase in the number of tunneling sites as the 7-His SAM thickness increases, following the deprotonation of histidine. Combined with the ultraviolet photoelectron spectroscopy (UPS) measurements, a modulable charge transport pathway through 7-His with imidazole groups of histidine as tunneling foot stones is revealed. Histidine therefore possesses a large potential for modulable functional (bio)electronic devices.
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