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Labeling DNA Probes

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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

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Published on: September 13, 2013

Peroxynitrite-Activated Conditional Chemical Probe for the Affinity-Based Protein Modification.

Chien-Chi Wu¹, Szu-Hsien Lee¹, Ting-Ju Huang¹

¹Department of Chemistry, National Tsing Hua University, 101 Section 2, Kuang-Fu Road, Hsinchu 300044, Taiwan.

Analytical Chemistry

|July 10, 2025

Summary

This summary is machine-generated.

We developed a new conditional-activated protein labeling probe that is activated by peroxynitrite. This probe enables specific labeling of human carbonic anhydrase (hCA) in cells and in vivo, and can detect peroxynitrite.

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Area of Science:

Chemical Biology
Biochemistry
Molecular Imaging

Background:

Affinity-based protein labeling relies on reactive electrophiles, which can cause instability and non-specific labeling.
Existing probes often lack stability and selectivity in complex biological systems.

Purpose of the Study:

To develop a conditional-activated affinity-based protein labeling strategy.
To create a probe activated by peroxynitrite for specific protein modification.
To enable detection of peroxynitrite in biological systems.

Main Methods:

Synthesized a probe with a peroxynitrite-responsive acyl hydrazide, Cy5 dye, and sulfonamide ligand for human carbonic anhydrase (hCA).
Tested probe activation and labeling specificity in living cells and in vivo.
Evaluated probe's ability to detect peroxynitrite secreted from macrophage cells.

Main Results:

Achieved specific and rapid labeling of hCA in the presence of peroxynitrite in cells and in vivo.
Demonstrated long-term in vivo imaging of the target protein due to stable covalent bond formation.
Showed the probe can detect peroxynitrite secreted by macrophage cells.
Highlighted the probe's ease of synthesis and resistance to hydrolysis compared to previous probes.

Conclusions:

The conditional-activated probe offers a stable and selective method for protein labeling under oxidative stress.
This new reagent is valuable for studying protein modification in biological environments with peroxynitrite.
The probe serves a dual purpose for both protein labeling and peroxynitrite detection.