Beilstein J. Org. Chem.2014,10, 660–666, doi:10.3762/bjoc.10.58
right-handed helical conformation.
Keywords: conformation; dehydroalanine; dehydropeptide; dehydrophenylalanine; NMR; Introduction
Structurally modified peptides are becoming increasingly interesting as potential substances with pharmacological effects [1]. Dehydropeptides are one representative of
the whole dehydropeptide [4][5][6][7]. It is noteworthy that the introduction of dehydroamino acid residues has a strong influence on the conformational preference of the peptide chain, irrespective of other constraints. The introduction of (Z)-dehydrophenylalanine stabilizes a β-turn conformation
dehydroalanine and dehydrophenylalanine residues. Therefore, we decided to check the influence of the introduction of a L-Val residue at different positions of dehydropeptides containing dehydroalanine and dehydrophenylalanine residues as well as two highly flexible glycine residues. We decided that the
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Graphical Abstract
Figure 1:
Sequences of the investigated dehydropeptides.