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Tagging and Fusion Proteins

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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

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Updated: Sep 11, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

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Red-Light-Induced Cysteine Modifications Suitable for Protein Labeling.

Tomasz Wdowik¹, Egor Fedorov¹, Tina-Thien Ho^2,3

¹Institute of Organic Chemistry, Polish Academy of Sciences, Kasprzaka 44/52, Warsaw 01-224, Poland.

ACS Organic & Inorganic Au

|August 11, 2025

Summary

This summary is machine-generated.

This study introduces a new method for bioconjugation using red light and a porphyrin catalyst, enabling efficient cysteine modification in biological settings. The technique offers a mild, aqueous-based approach for selective cysteine transformations in proteins.

Keywords:

bioconjugation cysteine photocatalysis porphyrin proteins red light thiol–ene reaction

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Area of Science:

Bioconjugation Chemistry
Photocatalysis
Protein Modification

Background:

Cysteine is a key amino acid for bioconjugation due to its thiol-ene reactivity.
Existing bioconjugation methods often require harsh conditions (UV light, initiators, heavy metals), limiting biological applications.
There is a need for mild, efficient, and selective cysteine modification techniques compatible with biological environments.

Purpose of the Study:

To develop a photocatalyzed thiol-ene radical reaction for cysteine bioconjugation.
To overcome the limitations of existing methods by using mild reaction conditions and red light.
To demonstrate the applicability of the method in aqueous media and for complex biological samples.

Main Methods:

Utilized a porphyrin-based photocatalyst.
Employed low-energy red light for photoinitiation.
Performed thiol-ene radical reactions in aqueous media.
Investigated selective transformations of free cysteine and cysteine residues in proteins.

Main Results:

Successfully demonstrated a photocatalyzed thiol-ene radical reaction under mild conditions.
The method employs a porphyrin catalyst and red light, avoiding UV radiation and heavy metals.
Achieved selective bioconjugation of cysteine in aqueous solutions and within complex protein structures.
The reaction could be expanded to a cysteinyl desulfurization reaction.

Conclusions:

Developed a versatile and mild bioconjugation strategy for cysteine using red-light photocatalysis.
This approach enhances the toolbox for modifying cysteine residues in biological systems.
The method's compatibility with aqueous media and complex proteins broadens its utility in biochemical research and applications.