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α-Helicomimetic foldamers as electron transfer mediators


α-Helical peptides are known as efficient mediators of electron transfer, however their use is limited to compounds longer that 7-10 residues. To overcome this limitation α-helicomimetic foldamers, based on oligourea backbone with general formula [-CH(R)-CH2-NH-CO-NH]n, were synthesized. Oligoureas are known to adopt robust 2.5-helical conformation where only four residues are enough to form stable 1.5 helical turns. This feature makes them great models to study the charge transfer process and the dependence of the mechanism of electron transition on the length of the mediator. Two families of different chain length (2, 4, 6 residues) oligoureas were synthesized with thiol group attached to δ+ or δ- helix dipole pole. This enables the adsorption of the molecules onto gold surface leading to formation of self-assembled monolayers. The helicity of compounds were confirmed in solution and in the solid state. Such systems were used to study the electron transfer process by current sensing atomic force microscopy (CS-AFM). The results showed that oligoureas may act as electron transfer mediators. Additionally, it was shown by the increasing force applied to the AFM tip, that oligourea helix is more stable than the helix formed by peptides.

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Publication details

The article was received on 17 Jul 2017, accepted on 04 Sep 2017 and first published on 05 Sep 2017

Article type: Paper
DOI: 10.1039/C7NR05209J
Citation: Nanoscale, 2017, Accepted Manuscript
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    α-Helicomimetic foldamers as electron transfer mediators

    K. Pulka-Ziach and S. Sęk, Nanoscale, 2017, Accepted Manuscript , DOI: 10.1039/C7NR05209J

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