Native chemical ligation (NCL), the most common form of chemical ligation, has become a widely used chemoselective technique to synthesize large peptides based on a capture/rearrangement concept. NCL has been extensively studied in peptidic compounds bearing a cysteine residue at the N terminus. Modified cysteine scaffolds have also been incorporated for the syntheses of novel peptides and proteins and for surface immobilization. The classical NCL method is limited to peptides possessing an N-terminal cysteine residue. To overcome this requirement of a specifically placed cysteine residue one approach is the use of thiol ligation auxiliaries, but unfortunately, removable cysteine mimics can sterically hinder ligation and difficulties can arise at the stage of auxiliary removal.We have successfully developed novel approach applying S to N long-range acyl migration to synthesize peptide and peptide analogs and also provided mechanistic evidence for the ligation process. A series of novel S-acyl peptides containing �- and/or ?-amino acid residues, which are useful intermediates in various synthetic and biological applications, were synthesized according to original protocols.

Development of novel strategies for coupling of peptide fragments utilizing S to N long-range acyl migration in isopeptide

248th National Meeting (2014)

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