Document Type
Article
Publication Date
4-16-2018
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.
Publication Title
Soft Matter
Volume
14
Issue
18
First Page
3528
Last Page
3535
Funder
Electrochemical Society Young Investigator Fellowship
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.
Recommended Citation
Su, Zihang; Pramounmat, Nuttanit; and Renner, Julie N., "Engineered Interaction Between Short Elastin-Like Peptides and Perfluorinated Sulfonic-Acid Ionomer" (2018). Faculty Scholarship. 63.
https://commons.case.edu/facultyworks/63
Comments
This is the Accepted Manuscript version of the article which has been published in final form at https://doi.org/10.1039/C8SM00351C.