Modification of N-terminal α-amine of proteins via biomimetic ortho-quinone-mediated oxidation

Siyao Wang, Qingqing Zhou, Xiaoping Chen, Rong-Hua Luo, Yunxue Li, Xinliang Liu, Liu-Meng Yang, Yong-Tang Zheng () and Ping Wang ()
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Siyao Wang: Shanghai Jiao Tong University
Qingqing Zhou: Shanghai Jiao Tong University
Xiaoping Chen: Shenzhen University
Rong-Hua Luo: Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming
Yunxue Li: Shanghai Jiao Tong University
Xinliang Liu: Shanghai Jiao Tong University
Liu-Meng Yang: Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming
Yong-Tang Zheng: Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming
Ping Wang: Shanghai Jiao Tong University

Nature Communications, 2021, vol. 12, issue 1, 1-9

Abstract: Abstract 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.

Date: 2021
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DOI: 10.1038/s41467-021-22654-7

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