摘要
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.
基金
supported by Guangdong Natural Science Funds for Distinguished Young Scholar (2018B030306017)
the 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)。
