Guo Tianyun, Wang Hong, Wang Chuang, Tang Shouchu, Liu Jian, Wang Xiaolei
State Key Laboratory of Applied Organic Chemistry, School of Pharmacy, Lanzhou University, Lanzhou 730000, P. R. China.
School of Environmental and Chemical Engineering, Lanzhou Resources & Environment Voc-Tech College, Lanzhou 730021, P. R. China.
J Org Chem. 2022 May 20;87(10):6852-6859. doi: 10.1021/acs.joc.2c00524. Epub 2022 May 10.
Post-translational modifications of proteins based on the amino acid residue dehydroalanine (Dha) have been widely adopted in molecular biology to expand their structural and functional capabilities. However, the construction of highly important amide C(sp)-C(sp) linkages on peptides through cross-coupling remains unexplored. In this article, we describe a photoredox-catalyzed C(sp) amidation that enables the mutation of Dha to an asparagine (Asn) motif. This amide installation strategy reported herein will guide us to create more additional derivatives of peptides, which may elucidate the mode of action and address an important area of unmet medical need.
基于氨基酸残基脱氢丙氨酸（Dha）的蛋白质翻译后修饰已在分子生物学中广泛应用，以扩展其结构和功能。然而，通过交叉偶联在肽上构建高度重要的酰胺C(sp)-C(sp)键仍未得到探索。在本文中，我们描述了一种光氧化还原催化的C(sp)酰胺化反应，该反应可将Dha突变为天冬酰胺（Asn）基序。本文报道的这种酰胺安装策略将指导我们创造更多的肽衍生物，这可能有助于阐明作用模式，并解决一个重要的未满足医疗需求领域。
