Date of Award

2018

Document Type

Dissertation/Thesis

Submission Date

October 2026

Thesis/Dissertation Advisor [Chair]

Carroll, Kate

Abstract

Reactive oxygen species (ROS) have traditionally been viewed as a harmful consequence of oxygen metabolism. However, scientists have discovered that ROS may oxidize cysteine residues of proteins, yielding sulfenic acid residues. This redox-mediated post-translational modification plays a significant biological role in cellular signaling, growth, and homeostasis. These processes were difficult to monitor in the past due to the lack of methods which can efficiently detect the changing redox states of cysteine residues. However, even with the advent of small molecule probes which selectively bind to oxidized cysteine residues, there is still work to be done in designing a more efficient probe, particularly for the sulfenic acid oxoform. Additionally, a probe that can characteristically fluoresce upon reacting with sulfenic acids would be extremely useful in biological imaging. Herein I describe a selective, reactive, and fluorogenic probe which can be used to detect protein sulfenylation.

Comments

Includes bibliography.

Extent

45 p.

Identifier

FAUHT00057

Download

Share

COinS