Format

Send to

Choose Destination
Biotechnol Bioeng. 2016 Feb;113(2):453-6. doi: 10.1002/bit.25720. Epub 2015 Sep 4.

Electrochemical activation of engineered protein switches.

Author information

1
Department of Chemical and Biomolecular Engineering, Johns Hopkins University, 3400 N. Charles St., Baltimore, Maryland, 21218.
2
Department of Materials Science and Engineering, Johns Hopkins University, 3400 N. Charles St., Baltimore, Maryland, 21218. oster@jhu.edu.
3
Department of Materials Science and Engineering, Johns Hopkins University, 3400 N. Charles St., Baltimore, Maryland, 21218.

Abstract

Engineered protein switches have a large dynamic range, high specificity for the activating ligand, and a modular architecture, and have been explored for a wide range of applications including biosensors and therapeutics. The ability to externally control switch function is important in extending applications for protein switches. We recently demonstrated that the on/off state could be controlled by the redox state of disulfide bonds introduced into the switches at select locations. Here, we demonstrate that an electrochemical signal can be used as an exogenous input to control switch function via reduction of the engineered disulfide bonds. This study suggests that disulfide-containing protein switch is a potentially useful platform for bioelectronic sensors with remote control of the sensing ability.

KEYWORDS:

allostery; disulfide bond; electrochemical reduction; protein engineering; protein switch

PMID:
26241391
PMCID:
PMC4721505
DOI:
10.1002/bit.25720
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Wiley Icon for PubMed Central
Loading ...
Support Center