Cross-linking furan-modified kisspeptin-10 to the KISS receptor
- Author
- Willem Vannecke (UGent) , Christophe Ampe (UGent) , Marleen Van Troys (UGent) , Massimiliano Beltramo and Annemieke Madder (UGent)
- Organization
- Abstract
- Chemical cross-linking is well-established for investigating protein-protein interactions. Traditionally, photo cross-linking is used but is associated with problems of selectivity and UV toxicity in a biological context. We here describe, with live cells and under normal growth conditions, selective cross-linking of a furan-modified peptide ligand to its membrane-presented receptor with zero toxicity, high efficiency, and spatio-specificity. Furan-modified kisspeptin-10 is covalently coupled to its glycosylated membrane receptor, GPR54(KISS1R). This newly expands the applicability of furan-mediated cross-linking not only to proteinprotein cross-linking but also to cross-linking in situ. Moreover, in our earlier reports on nucleic acid interstrand cross-linking, furan activation required external triggers of oxidation (via addition of N-bromo succinimide or singlet oxygen). In contrast, we here show, for multiple cell lines, the spontaneous endogenous oxidation of the furan moiety with concurrent selective cross-link formation. We propose that reactive oxygen species produced by NADPH oxidase (NOX) enzymes form the cellular source establishing furan oxidation.
- Keywords
- PROTEIN-COUPLED RECEPTOR, MASS-SPECTROMETRY, REACTIVE OXYGEN, BIOORTHOGONAL CHEMISTRY, NOX ENZYMES, INTERACTING PROTEINS, PHOTOAFFINITY PROBES, MAMMALIAN-CELLS, NADPH OXIDASE, LIVING CELLS
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-8527538
- MLA
- Vannecke, Willem, et al. “Cross-Linking Furan-Modified Kisspeptin-10 to the KISS Receptor.” ACS CHEMICAL BIOLOGY, vol. 12, no. 8, 2017, pp. 2191–200, doi:10.1021/acschembio.7b00396.
- APA
- Vannecke, W., Ampe, C., Van Troys, M., Beltramo, M., & Madder, A. (2017). Cross-linking furan-modified kisspeptin-10 to the KISS receptor. ACS CHEMICAL BIOLOGY, 12(8), 2191–2200. https://doi.org/10.1021/acschembio.7b00396
- Chicago author-date
- Vannecke, Willem, Christophe Ampe, Marleen Van Troys, Massimiliano Beltramo, and Annemieke Madder. 2017. “Cross-Linking Furan-Modified Kisspeptin-10 to the KISS Receptor.” ACS CHEMICAL BIOLOGY 12 (8): 2191–2200. https://doi.org/10.1021/acschembio.7b00396.
- Chicago author-date (all authors)
- Vannecke, Willem, Christophe Ampe, Marleen Van Troys, Massimiliano Beltramo, and Annemieke Madder. 2017. “Cross-Linking Furan-Modified Kisspeptin-10 to the KISS Receptor.” ACS CHEMICAL BIOLOGY 12 (8): 2191–2200. doi:10.1021/acschembio.7b00396.
- Vancouver
- 1.Vannecke W, Ampe C, Van Troys M, Beltramo M, Madder A. Cross-linking furan-modified kisspeptin-10 to the KISS receptor. ACS CHEMICAL BIOLOGY. 2017;12(8):2191–200.
- IEEE
- [1]W. Vannecke, C. Ampe, M. Van Troys, M. Beltramo, and A. Madder, “Cross-linking furan-modified kisspeptin-10 to the KISS receptor,” ACS CHEMICAL BIOLOGY, vol. 12, no. 8, pp. 2191–2200, 2017.
@article{8527538, abstract = {{Chemical cross-linking is well-established for investigating protein-protein interactions. Traditionally, photo cross-linking is used but is associated with problems of selectivity and UV toxicity in a biological context. We here describe, with live cells and under normal growth conditions, selective cross-linking of a furan-modified peptide ligand to its membrane-presented receptor with zero toxicity, high efficiency, and spatio-specificity. Furan-modified kisspeptin-10 is covalently coupled to its glycosylated membrane receptor, GPR54(KISS1R). This newly expands the applicability of furan-mediated cross-linking not only to proteinprotein cross-linking but also to cross-linking in situ. Moreover, in our earlier reports on nucleic acid interstrand cross-linking, furan activation required external triggers of oxidation (via addition of N-bromo succinimide or singlet oxygen). In contrast, we here show, for multiple cell lines, the spontaneous endogenous oxidation of the furan moiety with concurrent selective cross-link formation. We propose that reactive oxygen species produced by NADPH oxidase (NOX) enzymes form the cellular source establishing furan oxidation.}}, author = {{Vannecke, Willem and Ampe, Christophe and Van Troys, Marleen and Beltramo, Massimiliano and Madder, Annemieke}}, issn = {{1554-8929}}, journal = {{ACS CHEMICAL BIOLOGY}}, keywords = {{PROTEIN-COUPLED RECEPTOR,MASS-SPECTROMETRY,REACTIVE OXYGEN,BIOORTHOGONAL CHEMISTRY,NOX ENZYMES,INTERACTING PROTEINS,PHOTOAFFINITY PROBES,MAMMALIAN-CELLS,NADPH OXIDASE,LIVING CELLS}}, language = {{eng}}, number = {{8}}, pages = {{2191--2200}}, title = {{Cross-linking furan-modified kisspeptin-10 to the KISS receptor}}, url = {{http://doi.org/10.1021/acschembio.7b00396}}, volume = {{12}}, year = {{2017}}, }
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