Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
Protein sulfenylation (protein-SOH) is a central oxidation product of protein post-translational modification (PTM) that is crucial for signal transduction and cell behavior. However, the natural properties of protein-SOH, especially its low responsiveness and dynamic reversibility, pose a great challenge to the development of chemical probes to visualize protein-SOH . Here, we report an activated aggregation-induced emission (AIE) probe for specifically lighting-up protein-SOH . The AIE-active probe reacts with protein-SOH by nucleophilic substitution and exhibits intense fluorescence due to the restriction of intramolecular motion. The uniqueness of this probe ensures that fluorescence is only lighted up by protein-SOH, avoiding interference from small-molecule active substances and nonspecific adsorption of proteins. The significant increase of protein-SOH in atherosclerotic mice is detected by the AIE probe, and the level of protein-SOH positively correlates with atherosclerosis progression. Significantly, we find that specific binding of protein-SOH by this probe can inhibit plaque development, making it a promising therapeutic target. This study enables real-time imaging of protein oxidation modification , opening up a universal chemical tool for further elucidation of PTM and its role in signal transduction.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/acs.analchem.5c00911 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
AIE-Active Probe for Unveiling the Role of Protein Sulfenylation : Specific Imaging and Therapeutic Insights.
Anal Chem
June 2025
College of Chemistry, Chemical Engineering and Materials Science, Key Laboratory of Molecular and Nano Probes, Ministry of Education, Collaborative Innovation Center of Functionalized Probes for Chemical Imaging in Universities of Shandong, Institute of Molecular and Nano Science, Shandong Normal Un
Protein sulfenylation (protein-SOH) is a central oxidation product of protein post-translational modification (PTM) that is crucial for signal transduction and cell behavior. However, the natural properties of protein-SOH, especially its low responsiveness and dynamic reversibility, pose a great challenge to the development of chemical probes to visualize protein-SOH . Here, we report an activated aggregation-induced emission (AIE) probe for specifically lighting-up protein-SOH .
View Article and Find Full Text PDFSOHPRED: a new bioinformatics tool for the characterization and prediction of human S-sulfenylation sites.
Mol Biosyst
August 2016
Infection and Immunity Program, Biomedicine Discovery Institute and The Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia. and Monash Centre for Data Science, Faculty of Information Technology, Monash University, Clayton, VIC
Protein S-sulfenylation (SOH) is a type of post-translational modification through the oxidation of cysteine thiols to sulfenic acids. It acts as a redox switch to modulate versatile cellular processes and plays important roles in signal transduction, protein folding and enzymatic catalysis. Reversible SOH is also a key component for maintaining redox homeostasis and has been implicated in a variety of human diseases, such as cancer, diabetes, and atherosclerosis, due to redox imbalance.
View Article and Find Full Text PDFFormation, reactivity, and detection of protein sulfenic acids.
Chem Res Toxicol
November 2010
Department of Environmental Toxicology, University of California, Davis, California 95616, USA.
It has become clear in recent decades that the post-translational modification of protein cysteine residues is a crucial regulatory event in biology. Evidence supports the reversible oxidation of cysteine thiol groups as a mechanism of redox-based signal transduction, while the accumulation of proteins with irreversible thiol oxidations is a hallmark of stress-induced cellular damage. The initial formation of cysteine-sulfenic acid (SOH) derivatives, along with the reactive properties of this functional group, serves as a crossroads whereby the local redox environment may dictate the progression of either regulatory or pathological outcomes.
View Article and Find Full Text PDFProtein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation.
Biochemistry
November 1999
Department of Biochemistry, Wake Forest University Medical Center, Winston-Salem, North Carolina 27157, USA.
While it has been known for more than 20 years that unusually stable cysteine-sulfenic acid (Cys-SOH) derivatives can be introduced in selected proteins by mild oxidation, only recently have chemical and crystallographic evidence for functional Cys-SOH been presented with native proteins such as NADH peroxidase and NADH oxidase, nitrile hydratase, and the hORF6 and AhpC peroxiredoxins. In addition, Cys-SOH forms of protein tyrosine phosphatases and glutathione reductase have been suggested to play key roles in the reversible inhibition of these enzymes during tyrosine phosphorylation-dependent signal transduction events and nitrosative stress, respectively. Substantial chemical data have also been presented which implicate Cys-SOH in redox regulation of transcription factors such as Fos and Jun (activator protein-1) and bovine papillomavirus-1 E2 protein.
View Article and Find Full Text PDF