| 论文题目: | Modification of N-terminal Alpha-amine of Proteins Via Biomimetic Ortho-quinone-mediated Oxidation |
| 作者: | Siyao Wang, Qingqing Zhou, Xiaoping Chen, Rong-Hua Luo, Yunxue Li, Xinliang Liu, Liu-Meng Yang, Yong-Tang Zheng, Ping Wang |
| 联系作者: | zhengyt@mail.kiz.ac.cn; wangp1@sjtu.edu.cn |
| 发表年度: | 2021 |
| DOI: | DOI: 10.1038/s41467-021-22654-7 |
| 摘要: | Naturally abundant quinones are important molecules, which play essential roles in various biological processes due to their reduction potential. In contrast to their universality, the investigation of reactions between quinones and proteins remains sparse. Herein, we report the development of a convenient strategy to protein modification via a biomimetic quinone-mediated oxidation at the N-terminus. By exploiting unique reactivity of an ortho-quinone reagent, the alpha -amine of protein N-terminus is oxidized to generate aldo or keto handle for orthogonal conjugation. The applications have been demonstrated using a range of proteins, including myoglobin, ubiquitin and small ubiquitin-related modifier 2 (SUMO2). The effect of this method is further highlighted via the preparation of a series of 17 macrophage inflammatory protein 1 beta (MIP-1 beta) analogs, followed by preliminary anti-HIV activity and cell viability assays, respectively. This method offers an efficient and complementary approach to existing strategies for N-terminal modification of proteins. Methods for selective modification of the N-terminus of proteins are of high interest, but mostly require specific amino acid residues. Here, the authors report a selective and fast method for N-terminal modification of proteins based on quinone-mediated oxidation of the alpha-amine to aldehyde or ketone, and apply it to diverse proteins. |
| 刊物名称: | Nature Communications |
| 论文出处: | https://www.nature.com/articles/s41467-021-22654-7.pdf |
| 影响因子: | 12.121(2019年) |
