A selenoxide for single-atom protein modification of tyrosine residues enabled by water-resistant chalcogen and hydrogen bonding.

ABSTRACT: Post-translational modifications such as phosphorylation and acetylation are often minor structural modifications that can have profound effects on protein structure and thus broaden protein functions. Nevertheless, studying these effects directly is often out of reach because no general chemistry exists to introduce small modifications selectively; either a large, stable linker structure is selectively installed on protein residues, or a small substituent is introduced at the risk of low selectivity due to the use of reactive, indiscriminate molecules. Here we report a C-H functionalization reaction of tyrosine residues to access peptides and proteins modified by small structural changes including single-atom substitutions. A rationally designed selenoxide introduces a versatile selenoniu

SUBMITTER: Lin S 

PROVIDER: S-EPMC12411275 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature