Photocaged Activity-Based Probes for Spatiotemporal Detection of Protein S-sulfenylation in Living Cells

13 May 2022, Version 2
This content is a preprint and has not undergone peer review at the time of posting.


Protein cysteine residues have unique reactivity due to the low redox potential of its thiol side chain. Protein S-sulfenylation (protein sulfenic acid), as one of the most significant oxidative post-translational modifications (OxiPTMs), plays a vital role in regulating protein function. Due to the transient presence of sulfenic acid in living cell, many detecting methods have been limited. Activity-based probes provide powerful tools to elucidate this process, so their discovery has been at the forefront of redox biology. In this study, two caged cysteine sulfenic acid probes DYn-2-ONB, DYn-2-Cou with either an o-nitrobenzyl or coumarin protecting group were developed. Both probes can be efficiently uncaged via irradiation to produce the active C-nucleophile probe DYn-2. Labeling assay in living cells demonstrated DYn-2-ONB exhibited better labeling capacity compared with DYn-2, providing it as a powerful tool to detect protein S-sulfenylation in spatio-temporally controllable manner.


Sulfenic acid
Activity-based probe
Light activation
Spatiotemporal detection
Protein S-sulfenylation

Supplementary materials

SI-Photocaged SOH probes
The file contains experimental details, synthetic procedures, characterization data (NMR spectra; ESI mass spectra), etc.


Comments are not moderated before they are posted, but they can be removed by the site moderators if they are found to be in contravention of our Commenting Policy [opens in a new tab] - please read this policy before you post. Comments should be used for scholarly discussion of the content in question. You can find more information about how to use the commenting feature here [opens in a new tab] .
This site is protected by reCAPTCHA and the Google Privacy Policy [opens in a new tab] and Terms of Service [opens in a new tab] apply.