Stereoselective and Divergent Construction of β-Thiolated/Selenolated Amino Acids via Photoredox-Catalyzed Asymmetric Giese Reaction.

ABSTRACT: Sulfur and selenium occupy a distinguished position in biology owing to their redox activities, high nucleophilicity, and acyl transfer capabilities. Thiolated/selenolated amino acids, including cysteine, selenocysteine, and their derivatives, play critical roles in regulating the conformation and function of proteins and serve as an important motif for peptide design and bioconjugation. Unfortunately, a general and concise method to attain enantiopure β-thiolated/selenolated amino acids remains an unsolved problem. Herein, we present a photoredox-catalyzed asymmetric method for the preparation of enantiopure β-thiolated/selenolated amino acids using a simple chiral auxiliary, which controls the diastereoselectivity of the key alkylation step and acts as an orthogonal protecting group in t

SUBMITTER: Yin H 

PROVIDER: S-EPMC10249021 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature