Shanghai Key Laboratory for Molecular Engineering of Chiral Drugs, School of Chemistry and Chemical Engineering, Frontiers Science Center for Transformative Molecules, Shanghai Jiao Tong University, Shanghai, China.
Methods Mol Biol. 2022;2530:109-123. doi: 10.1007/978-1-0716-2489-0_8.
Thiolated/selenolated amino acids are irreplaceable despite their rare abundance in proteins. They play critical roles in regulating the conformation and function of proteins and peptide design as well as bioconjugation. Furthermore, β-thiolated/selenolated amino acids are important motifs in native chemical ligation-dechalcogenation strategy for protein synthesis. However, a universal method to access enantiopure β-thiolated/selenolated amino acids has not been reported. Herein, we developed a practical strategy for the preparation of a variety of enantiopure β-thiolated/selenolated amino acids via photoredox-catalyzed Giese reaction.
虽然硫代/硒代氨基酸在蛋白质中的丰度很少,但它们在调节蛋白质的构象和功能以及多肽设计和生物缀合方面起着至关重要的作用。此外,β-硫代/硒代氨基酸是天然化学连接-去硫策略中用于蛋白质合成的重要基序。然而,尚未报道获得对映纯β-硫代/硒代氨基酸的通用方法。在此,我们通过光氧化还原催化的 Giese 反应开发了一种实用的策略,用于制备各种对映纯的β-硫代/硒代氨基酸。