Red-light-induced cysteine modifications suitable for protein labeling
Red-light-induced cysteine modifications suitable for protein labeling
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.
bioconjugation, cysteine, photocatalysis, porphyrin, proteins, red light, thiol-ene reaction
Wdowik, Tomasz
7460f841-ab16-4621-bfc4-8fc6c97cdc29
Fedorov, Egor
0e43da80-393c-41e8-83de-eb555019cde5
Ho, Tina-Thien
6e29e0a9-751e-466e-8321-49f0325fccb9
Duriez, Patrick
4cf499bc-007a-43b3-b180-d6e5dc3d151b
Stulz, Eugen
9a6c04cf-32ca-442b-9281-bbf3d23c622d
Gryko, Dorota
67e6fcd5-0d54-4a5d-a93b-61d74251b661
6 August 2025
Wdowik, Tomasz
7460f841-ab16-4621-bfc4-8fc6c97cdc29
Fedorov, Egor
0e43da80-393c-41e8-83de-eb555019cde5
Ho, Tina-Thien
6e29e0a9-751e-466e-8321-49f0325fccb9
Duriez, Patrick
4cf499bc-007a-43b3-b180-d6e5dc3d151b
Stulz, Eugen
9a6c04cf-32ca-442b-9281-bbf3d23c622d
Gryko, Dorota
67e6fcd5-0d54-4a5d-a93b-61d74251b661
Wdowik, Tomasz, Fedorov, Egor, Ho, Tina-Thien, Duriez, Patrick, Stulz, Eugen and Gryko, Dorota
(2025)
Red-light-induced cysteine modifications suitable for protein labeling.
ACS Organic and Inorganic Au.
(doi:10.1021/acsorginorgau.5c00025).
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.
Text
wdowik-et-al-2025-red-light-induced-cysteine-modifications-suitable-for-protein-labeling
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More information
Accepted/In Press date: 3 April 2025
e-pub ahead of print date: 9 April 2025
Published date: 6 August 2025
Keywords:
bioconjugation, cysteine, photocatalysis, porphyrin, proteins, red light, thiol-ene reaction
Identifiers
Local EPrints ID: 501540
URI: http://eprints.soton.ac.uk/id/eprint/501540
ISSN: 2694-247X
PURE UUID: 4aa5b510-0389-4b4d-bd08-57dfc1d1fa69
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Date deposited: 03 Jun 2025 16:56
Last modified: 03 Sep 2025 01:41
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Contributors
Author:
Tomasz Wdowik
Author:
Egor Fedorov
Author:
Tina-Thien Ho
Author:
Patrick Duriez
Author:
Dorota Gryko
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