Bioorthogonal Probe BTD-Az Enables Sensitive and Rapid In Vivo Profiling of Protein Cysteine Sulfenylation.

ABSTRACT: Cysteine sulfenylation (Cys-SOH) is a transient redox-sensitive post-translational modification that regulates protein activity and cellular stress responses, yet its in vivo dynamics remain difficult to capture due to short half-life and low abundance. Here, we report the design and application of BTD-Az, a cell-permeable probe that incorporates an azide handle into the benzothiazine scaffold, enabling rapid bioorthogonal labeling of Cys-SOH both in vivo and in vitro, followed by efficient enrichment through strain-promoted azide-alkyne cycloaddition. This approach streamlines the detection and analysis of Cys-SOH with exceptional specificity and convenience. BTD-Az exhibited negligible cytotoxicity, efficiently enriched sulfenylated proteins in vitro, and achieved direct in vivo labeling

SUBMITTER: Xu M 

PROVIDER: S-EPMC12635961 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature