Diselenide–selenoester ligation for chemical protein synthesis

Site‐Selective Modification of Peptides and Proteins via Interception of Free‐Radical‐Mediated Dechalcogenation

“…[37] The development of diselenide-selenoester ligation (DSL) employs both selenium-containing fragments to enable rapid, additive-free peptide ligation. [38][39][40][41][42][43] Protocols that facilitate the post-ligation conversion of internal Cys and Sec residues to alanine (Ala), via desulfurization and deselenization, respectively, [44,45] permit peptide ligation at sites that contain this more abundant residue. Further developments in this field include the utilization of non-proteinogenic thiolated and selenolated residues, which, when coupled with dechalcogenation, [46,47] grant access to a broad range of ligation junctions, dramatically enhancing the scope of the technique.…”

“…Further developments to this powerful method [33] include the use of Sec‐containing peptides [34–36] and selenoester peptides to accelerate the ligation reaction [37] . The development of diselenide‐selenoester ligation (DSL) employs both selenium‐containing fragments to enable rapid, additive‐free peptide ligation [38–43] . Protocols that facilitate the post‐ligation conversion of internal Cys and Sec residues to alanine (Ala), via desulfurization and deselenization, respectively, [44, 45] permit peptide ligation at sites that contain this more abundant residue.…”

Site‐Selective Modification of Peptides and Proteins via Interception of Free‐Radical‐Mediated Dechalcogenation

“…[37] Thed evelopment of diselenideselenoester ligation (DSL) employs both selenium-containing fragments to enable rapid, additive-free peptide ligation. [38][39][40][41][42][43] Protocols that facilitate the post-ligation conversion of internal Cys and Sec residues to alanine (Ala), via desulfurization and deselenization, respectively, [44,45] permit peptide ligation at sites that contain this more abundant residue.F urther developments in this field include the utilization of non-proteinogenic thiolated and selenolated residues,w hich, when coupled with dechalcogenation, [46,47] grant access to ab road range of ligation junctions,dramatically enhancing the scope of the technique.…”

Chemical synthesis of a haemathrin sulfoprotein library reveals enhanced thrombin inhibition following tyrosine sulfation

“…Each of the peptides were then deprotected and cleaved from resin using an acidic cocktail followed by PMB deprotection (see ESI, † for full synthetic details). 28 The final step to generate the target C-terminal diselenide fragments involved deprotection of the nP sulfate ester(s). While these esters are normally cleaved through the treatment of nucleophilic azide or acetate reagents, 17,29 we found that these could be efficiently and cleanly deprotected by simply incubating the fragments in Gnd buffer at 50 1C for 2 hours.…”