Author ORCID Identifier

https://orcid.org/0000-0002-6140-4346

Document Type

Article

Publication Date

4-2021

DOI

10.1016/j.bej.2021.107933

Publication Title

Biochemical Engineering Journal

First Page

107933

Volume

168

College/School

Case School of Engineering

Department/Center

Chemical & Biomolecular Engineering

Grant

2018-68011-28691; 1739473

Funder

United States Department of Agriculture; National Science Foundation (NSF)

Abstract

Elastin-like peptides (ELPs) immobilized to solid surfaces have recently gained attention for use in electrochemical applications in sensing as well as bioenabled electrode assembly. Key to the success of these applications is understanding how ELPs impact the access and electron transfer of reacting species to the solid surface (effective surface coverage). In this study, short ELPs with varying hydrophobicity and sequence length were designed for gold attachment, and the effect on the ability of a redox probe to access a gold surface was characterized by cyclic voltammetry. A quantitative model describing the relationship between ELP effective surface coverage as a function of mean hydrophobicity and mass loading was elucidated based on the results, showing the ability to precisely control surface properties by tuning the ELP sequence. This model will be useful for the design of surface-bound ELP sequences that exhibit desired effective surface coverage for electrochemical as well as biomaterial applications.

Comments

This is an Accepted Manuscript of an article published by Elsevier in Biochemical Engineering Journal, available at: https://doi.org/10.1016/j.bej.2021.107933.

Available for download on Friday, February 10, 2023

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