Chemical- and photo-activation of protein-protein thiol-ene coupling for protein profiling
Abstract The thiol-ene reaction between an alkene and a thiol can be exploited for selective labelling of cysteine residues in protein profiling applications. Here, we explore thiol-ene activation in systems from chemical models to complex cellular milieus, using UV, visible wavelength and redox ini...
Saved in:
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2025-01-01
|
| Series: | Communications Chemistry |
| Online Access: | https://doi.org/10.1038/s42004-025-01412-6 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832571940557029376 |
|---|---|
| author | André Campaniҫo Marcin Baran Andrew G. Bowie Daniel B. Longley Timothy Harrison Joanna F. McGouran |
| author_facet | André Campaniҫo Marcin Baran Andrew G. Bowie Daniel B. Longley Timothy Harrison Joanna F. McGouran |
| author_sort | André Campaniҫo |
| collection | DOAJ |
| description | Abstract The thiol-ene reaction between an alkene and a thiol can be exploited for selective labelling of cysteine residues in protein profiling applications. Here, we explore thiol-ene activation in systems from chemical models to complex cellular milieus, using UV, visible wavelength and redox initiators. Initial studies in chemical models required an oxygen-free environment for efficient coupling and showed very poor activation when using a redox initiator. When thiol-ene activation was performed in protein and cell lysate models, all three initiation methods were successful. Faster thiol-ene reaction was observed as the cysteine and alkene were brought into proximity by a binding event prior to activation, leading to quicker adduct formation in the protein model system than the chemical models. Furthermore, in the protein-protein coupling, none of the activators required an oxygen-free environment. Taken together, these observations demonstrate the broad potential for thiol-ene coupling to be used in protein profiling. |
| format | Article |
| id | doaj-art-88258e1847d646f199c3660e90689a91 |
| institution | Kabale University |
| issn | 2399-3669 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Communications Chemistry |
| spelling | doaj-art-88258e1847d646f199c3660e90689a912025-02-02T12:12:13ZengNature PortfolioCommunications Chemistry2399-36692025-01-018111010.1038/s42004-025-01412-6Chemical- and photo-activation of protein-protein thiol-ene coupling for protein profilingAndré Campaniҫo0Marcin Baran1Andrew G. Bowie2Daniel B. Longley3Timothy Harrison4Joanna F. McGouran5School of Chemistry, Trinity College DublinSchool of Biochemistry and Immunology, Trinity College DublinSchool of Biochemistry and Immunology, Trinity College DublinThe Patrick G. Johnston Centre for Cancer Research, Queen’s University BelfastThe Patrick G. Johnston Centre for Cancer Research, Queen’s University BelfastSchool of Chemistry, Trinity College DublinAbstract The thiol-ene reaction between an alkene and a thiol can be exploited for selective labelling of cysteine residues in protein profiling applications. Here, we explore thiol-ene activation in systems from chemical models to complex cellular milieus, using UV, visible wavelength and redox initiators. Initial studies in chemical models required an oxygen-free environment for efficient coupling and showed very poor activation when using a redox initiator. When thiol-ene activation was performed in protein and cell lysate models, all three initiation methods were successful. Faster thiol-ene reaction was observed as the cysteine and alkene were brought into proximity by a binding event prior to activation, leading to quicker adduct formation in the protein model system than the chemical models. Furthermore, in the protein-protein coupling, none of the activators required an oxygen-free environment. Taken together, these observations demonstrate the broad potential for thiol-ene coupling to be used in protein profiling.https://doi.org/10.1038/s42004-025-01412-6 |
| spellingShingle | André Campaniҫo Marcin Baran Andrew G. Bowie Daniel B. Longley Timothy Harrison Joanna F. McGouran Chemical- and photo-activation of protein-protein thiol-ene coupling for protein profiling Communications Chemistry |
| title | Chemical- and photo-activation of protein-protein thiol-ene coupling for protein profiling |
| title_full | Chemical- and photo-activation of protein-protein thiol-ene coupling for protein profiling |
| title_fullStr | Chemical- and photo-activation of protein-protein thiol-ene coupling for protein profiling |
| title_full_unstemmed | Chemical- and photo-activation of protein-protein thiol-ene coupling for protein profiling |
| title_short | Chemical- and photo-activation of protein-protein thiol-ene coupling for protein profiling |
| title_sort | chemical and photo activation of protein protein thiol ene coupling for protein profiling |
| url | https://doi.org/10.1038/s42004-025-01412-6 |
| work_keys_str_mv | AT andrecampaniҫo chemicalandphotoactivationofproteinproteinthiolenecouplingforproteinprofiling AT marcinbaran chemicalandphotoactivationofproteinproteinthiolenecouplingforproteinprofiling AT andrewgbowie chemicalandphotoactivationofproteinproteinthiolenecouplingforproteinprofiling AT danielblongley chemicalandphotoactivationofproteinproteinthiolenecouplingforproteinprofiling AT timothyharrison chemicalandphotoactivationofproteinproteinthiolenecouplingforproteinprofiling AT joannafmcgouran chemicalandphotoactivationofproteinproteinthiolenecouplingforproteinprofiling |