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

ABSTRACT: Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (?(Z)Phe and ?Ala) 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-?Ala-Gly-?(Z)Phe-Val-OMe (3), which adopts a right-handed helical conformation.

SUBMITTER: Jewginski M

PROVIDER: S-EPMC3999861 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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

Jewgiński Michał M Krzciuk-Gula Joanna J Makowski Maciej M Latajka Rafał R Kafarski Paweł P

Beilstein journal of organic chemistry 20140314

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 con ...[more]

PMID: 24778717

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