ArticleACS organic & inorganic Au2025
Red-Light-Induced Cysteine Modifications Suitable for Protein Labeling.
Article in ACS organic & inorganic Au, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Selenoxanthylium Salts─Organic Photocatalysts for Low-Energy Photoredox Catalysis.Journal of the American Chemical Society · 2026Article
- An Initiator-Free Electrochemical Approach to Radical Thiol-Ene Coupling in a Microfluidic Reactor.Molecules (Basel, Switzerland) · 2026Article
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Authors and funding
6 authors.
Funding
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Abstract
The naturally low abundance of cysteine in proteins, combined with its propensity to undergo thiol-ene reactions, makes it a preferred amino acid for various bioconjugations. However, most of these methods rely on the use of UV radiation, radical initiators, or heavy-metal-based photocatalysts, which limits their applicability in complex biological environments. Herein, we report a photocatalyzed thiol-ene radical reaction that overcomes these limitations by employing a porphyrin-based photocatalyst and low-energy red light. This method operates under mild reaction conditions and can be expanded to a cysteinyl desulfurization reaction. As this approach proceeds in aqueous media and facilitates selective transformations of both simple free cysteine and cysteine residues within complex protein, it significantly expands the existing toolbox for cysteine bioconjugation.
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Registered trials
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