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 the subsequent peptide synthesis. Our protocol can be used to prepare a wide range of β-thiolated/selenolated amino acids on a gram scale, which would otherwise be difficult to obtain using conventional methods. The effect of our chemistry was further highlighted and validated through the preparation of a series of peptidyl thiol/selenol analogues, including cytochrome c oxidase subunit protein 7C and oxytocin.