Double helices are not common in polypeptides and proteins except in the peptide antibiotic gramicidin A and analogous l,d-peptides. In contrast to natural polypeptides, remarkable β-double-helical structures from achiral γ-peptides built from α,β-unsaturated γ-amino acids have been observed. The crystal structures suggest that they adopted parallel β-double helical structures and these structures are stabilized by the interstrand backbone amide H-bonds. Furthermore, both NMR spectroscopy and fluorescence studies support the existence of double-helical conformations in solution. Although a variety of folded architectures featuring distinct H-bonds have been discovered from the β- and γ-peptide foldamers, this is the first report to show that achiral γ-peptides can spontaneously intertwine into β-double helical structures.
Keywords: achirality; amino acids; foldamers; peptides; β-double helix.
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