期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 21, 期 47, 页码 26058-26065出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9cp04695j
关键词
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资金
- National Natural Science Foundation of China [21773169, 21872103, 21973069]
- National Key RD Program [2017YFA0204503, 2016YFB0401100]
- PEIYANG Young Scholars Program of Tianjin University [2018XRX-0007]
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 beta = similar to 0.5 angstrom(-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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