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Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (Δ(Z)Phe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of peptides is discussed. The obtained results suggest that the strongest influence on the conformation of peptides arises from a valine residue inserted at the C-terminal position. The most ordered conformation was found for peptide Boc-Gly-ΔAla-Gly-Δ(Z)Phe-Val-OMe (3), which adopts a right-handed helical conformation.

Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine