Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 3 and 5 in peptide chain

Synthesis and structural studies of hexapeptides containing two dehydroamino acid residues in positions 3 and 5 in a peptide chain were performed. All the investigated peptides adopted bent conformations, stabilized by intramolecular hydrogen bonding, and could exist as two different conformers in solution. Only in the case of the peptide containing ΔAla residues, expected 310-helical conformation was found.