Selenocysteine-mediated backbone cyclization of unprotected peptides followed by alkylation, oxidative elimination or reduction of the selenol

Abstract

An unprotected 16 residue peptide containing a C-terminal thioester and an N-terminal selenocysteine residue efficiently cyclizes in the presence of thiophenol; subsequent reduction, elimination or alkylation of the selenol yields modified cyclic peptides with alanine, dehydroalanine or a non-natural amino acid at the site of ligation.