期刊
SCIENCE CHINA-CHEMISTRY
卷 65, 期 7, 页码 1356-1361出版社
SCIENCE PRESS
DOI: 10.1007/s11426-022-1252-7
关键词
lysine; protein modification; single-site modification; stapling
资金
- Guangdong Natural Science Funds for Distinguished Young Scholar [2018B030306017]
- National Natural Science Foundation of China [22077144]
- Guangdong Provincial Key Laboratory of Chiral Molecule and Drug Discovery [2019B030301005]
- Key Research and Development Program of Guangdong Province [2020B1111110003]
Site-selective modification of peptides/proteins is a crucial method for studying post-translational modifications, chemical biology, and drug development. In this study, a visible-light-driven and Cys-directed Lys site-selective stapling approach was developed, enabling selective modification and multi-functionalization.
Site-selective modification of peptide/protein is a vital approach to disclose post-translational modifications (PTMs) and plays a crucial role in chemical biology, as well as drug development. Compared with synthetic and chemical biology methods, chemical modification of native peptide/protein provides a more versatile approach to achieve late-stage diversification for functional studies. Lysine featured high nucleophilicity, frequency, and solvent accessibility, making its site-selective modification important but elusive. Herein, we reported a visible-light-driven and Cys-directed Lys site-selective stapling approach for peptide/protein. By cleavable Cys anchoring, site-selective Lys single-site modification was achieved, and this method could be applied to multi-functionalization.
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