Controlled Reversible N-Terminal Modification of Peptides and Proteins

• DOI: 10.1021/jacs.4c04894
• Publication Date: 2024-08-15T07:50:50Z
• Authors: Zeng Lin; Bo Liu; Mengru Lu; Yongqin Wang; Xuelian Ren; Zhaoxi Liu; Caili Luo; Wei Shi; Xiangman Zou; Xiaohan Song; Feng Tang; He Huang; Wei Huang
• Keywords: Posttranslational modification; Chemical modification; Chemical Biology

A reversible modification strategy enables a switchable cage/decage process of proteins with an array applications for protein function research. However, general N-terminal selective strategies which present site selectivity are specifically limited. Herein, we report compatible 20 canonical amino acids at the by palladium-catalyzed cinnamylation native peptides and under biologically relevant conditions. This approach broadens substrate adaptability shows potential impact on more challenging substrates such as antibodies. In presence 1,3-dimethylbarbituric acid, deconjugation released efficiently. Harnessing nature this protocol, practical were demonstrated precise modulation antibodies traceless enrichment protein-of-interest proteomics analysis. novel on/off working N-terminus will provide new opportunities in chemical biology medicinal