Phase-transfer conditions permit facile introduction of dichlorotetrazine into unprotected peptides and proteins between two cysteine sulfhydryls (i.e., stapled). This method enables the rapid construction of a diverse set of peptide macrocycles, varying in size and functionally. In turn, the photolabile S,S-tetrazine bridge can be removed (i.e., unstapled) with a biocompatible light source to release the restricted conformation. Treatment of the dithiocyanate products with cysteine will regenerate the native peptide/protein structures.

Peptide/protein stapling and un-stapling: Phase-transfer introduction of s-tetrazine into unprotected peptides/proteins, photochemical release, and regeneration of the native structures

248th National Meeting (2014)

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