Tetrazine ligation for chemical proteomics

Proteome Science

Review

Jongmin Park¹  Kyungtae Kang²  Eunha Kim³ 

[1] Center for Systems Biology, Massachusetts General Hospital, Harvard Medical School, 185 Cambridge St, CPZN 5206, 02114, Boston, Massachusetts, USA;Department of Applied Chemistry, Kyung Hee University, 17104, Yongin, Gyeonggi, Republic of Korea;Department of Molecular Science and Technology, Ajou University, 16499, Suwon, Republic of Korea;

关键词: iEDDA reaction;    Bioorthogonal reaction;    Tetrazine;    Chemical biology;    Chemical proteomics;   

DOI  :  10.1186/s12953-017-0121-5

 received in 2017-02-19, accepted in 2017-06-15,  发布年份 2017

来源: Springer

【 摘 要 】

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.

【 授权许可】

CC BY   
© The Author(s). 2017