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Wang Ping’s Team Reported Protein Modification via Biomimetic Quinone-mediated Oxidation

May 12, 2021      Author:

Site-specific modification of protein is to modify the specific site of protein through chemical reaction, so as to achieve a series of purposes such as modifying or labeling protein. The site-specific modification of protein requires strict reaction conditions: the reaction needs to be carried out in aqueous solution, and other side-chain groups of protein do not participate in the reaction. The research team led by Wang Ping, a special researcher of Shanghai Jiao Tong University, has been devoted to the chemical synthesis and modification of protein and peptides. Recently, the research group cooperated with Zheng Yongtang, researcher of Kunming Institute of Zoology, Chinese Academy of Sciences, and developed a method for selectively modifying the N- terminal of proteins via biomimetic ortho-quinone-mediated oxidation, which was further applied to various fields including protein labeling and anti-HIV drug screening.

The work was published in Nature Communications under the title of "Modification of N-terminal α-amine of proteins via biomimetic ortho-quinone-mediated oxidation". SJTU special researcher Wang Ping, and Zheng Yongtang, a researcher at Kunming Institute of Zoology, CAS, are the co-corresponding authors of this research paper; Wang Siyao, Zhou Qingqing, Chen Xiaoping and Luo Ronghua are co-first authors. Wang Siyao, one of the first authors, joined Wang Ping's team in SJTU School of Chemistry and Chemical Engineering as a post doctorate after graduating from the School of Chemistry, University of Sydney, Australia. He has received a fund from the Postdoctoral International Exchange Program. This work is also supported by the National Natural Science Foundation of China.


Source: School of Chemistry and Chemical Engineering, SJTU

Translated by Zhou Rong

Proofread by Xiao Yangning, Fu Yuhe



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 α-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 1β (MIP-1β) 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.