title: Peptide/protein stapling and unstapling: introduction of s-tetrazine, photochemical release, and regeneration of the peptide/protein.
abstract: Protocols have been achieved that permit facile introduction of s-tetrazine into unprotected peptides and the protein, thioredoxin, between two cysteine sulfhydryl groups (i.e., staple), followed by photochemical release (i.e., unstaple) and regeneration of the peptide/protein upon removal of the cyano groups from the derived bisthiocyanate. The S,S-tetrazine macrocycles in turn provide a convenient handle for probe introduction by exploiting the inverse electron demand Diels-Alder reactivity of the tetrazine.
authors: Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
authors: Stephen P
authors: SP
authors: Brown
authors: Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
authors: Amos B
authors: AB
authors: Smith
mesh_terms: D000595:Amino Acid Sequence; D061565:Cycloaddition Reaction; D003545:Cysteine / Q000737:chemistry*; D006573:Heterocyclic Compounds, 1-Ring / Q000737:chemistry*; D047028:Macrocyclic Compounds / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry; D013879:Thioredoxins / Q000737:chemistry*
chemical_list: D006573:Heterocyclic Compounds, 1-Ring; D047028:Macrocyclic Compounds; D010455:Peptides; D013438:Sulfhydryl Compounds; D013879:Thioredoxins; D003545:Cysteine