Author ORCID Identifier

Zihang Su

Julie N. Renner

Document Type

Article

Publication Date

4-16-2018

Publication Title

Soft Matter

First Page

3528

Last Page

3535

Volume

14

Issue

18

College/School

Case School of Engineering

Funder

Electrochemical Society Young Investigator Fellowship

Abstract

Control of ionomer thin films on metal surfaces is important for a range of electrodes used in electrochemical applications. Engineered peptides have emerged as powerful tools in electrode assembly because binding sites and peptide structures can be modulated by changing the amino acid sequence. However, no studies have been conducted showing peptides can be engineered to interact with ionomers and metals simultaneously. In this study, we design a single-repeat elastin-like peptide to bind to gold using a cysteine residue, and bind to a perfluorinated sulfonic-acid ionomer called Nafion® using a lysine guest residue. Quartz crystal microbalance with dissipation monitoring and atomic force microscopy are used to show that an elastin-like peptide monolayer attached to gold facilitates the formation of a thin, phase-separated ionomer layer. Dynamic light scattering confirms that the interaction between the peptide with the lysine residue and the ionomer also happens in solution, and circular dichroism shows that the peptides maintain their secondary structures in the presence of ionomer. These results demonstrate that elastin-like peptides are promising tools for ionomer control in electrode engineering.

Rights

This article may be used for non-commercial purposes in accordance with the Royal Society of Chemistry's Non-commerical terms of use of information.

Comments

This is the Accepted Manuscript version of the article which has been published in final form at https://doi.org/10.1039/C8SM00351C.

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