期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 24, 期 47, 页码 28878-28885出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d2cp02807g
关键词
-
资金
- NSFC [21974102, 21705019]
- Weizmann Institute
- Israel Science Foundation
- Kimmelman Center for Biomolecular Structure and Assembly
- Katzir-Makineni Chair in Chemistry
The solid-state electron transport properties of oligopeptide junctions can be modulated by charges and internal hydrogen bonding. Inserting a Tyr residue into the peptides enhances the conductivity of the junctions, while deprotonation of the Tyr-containing peptides further increases the efficiency of electron transport. The increase in conductance upon deprotonation is mainly due to enhanced coupling between the charged C-terminus carboxylate group and the adjacent Au electrode.
A way of modulating the solid-state electron transport (ETp) properties of oligopeptide junctions is presented by charges and internal hydrogen bonding, which affect this process markedly. The ETp properties of a series of tyrosine (Tyr)-containing hexa-alanine peptides, self-assembled in monoIayers and sandwiched between gold electrodes, are investigated in response to their protonation state. Inserting a Tyr residue into these peptides enhances the ETp carried via their junctions. Deprotonation of the Tyr-containing peptides causes a further increase of ETp efficiency that depends on this residue's position. Combined results of molecular dynamics simulations and spectroscopic experiments suggest that the increased conductance upon deprotonation is mainly a result of enhanced coupling between the charged C-terminus carboxylate group and the adjacent Au electrode. Moreover, intra-peptide hydrogen bonding of the Tyr hydroxyl to the C-terminus carboxylate reduces this coupling. Hence, the extent of such a conductance change depends on the Tyr-carboxylate distance in the peptide's sequence.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据