Conformation of dehydropentapeptides containing four achiral amino acid residues - controlling the role of L-valine.
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.
Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland.
Michał
M
Jewgiński
Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland.
Joanna
J
Krzciuk-Gula
Faculty of Chemistry, University of Opole, Oleska 48, 45-052 Opole, Poland.
Maciej
M
Makowski
Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland.
Rafał
R
Latajka
Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland.
Paweł
P
Kafarski
NMR; conformation; dehydroalanine; dehydropeptide; dehydrophenylalanine