Tetrazine ligation for chemical proteomics |
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| Authors: | Kyungtae Kang Jongmin Park Eunha Kim |
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| Affiliation: | 1.Department of Applied Chemistry,Kyung Hee University,Yongin,Republic of Korea;2.Center for Systems Biology,Massachusetts General Hospital, Harvard Medical School,Boston,USA;3.Department of Molecular Science and Technology,Ajou University,Suwon,Republic of Korea |
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| Abstract: | Determining small molecule—target protein interaction is essential for the chemical proteomics. One of the most important keys to explore biological system in chemical proteomics field is finding first-class molecular tools. Chemical probes can provide great spatiotemporal control to elucidate biological functions of proteins as well as for interrogating biological pathways. The invention of bioorthogonal chemistry has revolutionized the field of chemical biology by providing superior chemical tools and has been widely used for investigating the dynamics and function of biomolecules in live condition. Among 20 different bioorthogonal reactions, tetrazine ligation has been spotlighted as the most advanced bioorthogonal chemistry because of their extremely faster kinetics and higher specificity than others. Therefore, tetrazine ligation has a tremendous potential to enhance the proteomic research. This review highlights the current status of tetrazine ligation reaction as a molecular tool for the chemical proteomics. |
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