Publication Date:
2014-03-15
Description:
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. Beilstein J. Org. Chem. 2014, 10, 660–666. doi:10.3762/bjoc.10.58
Keywords:
conformationdehydroalaninedehydropeptidedehydrophenylalanineNMR
Electronic ISSN:
1860-5397
Topics:
Chemistry and Pharmacology
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