Another approach to developing improved peptide-based drugs in our group is to identify extended sequences of β- and γ-amino acids that can be incorporated into α-helical coiled coil-based sequences to produce artificial chimeric folding motifs. Such artificial motifs, by virtue of their orthogonal structural elements, may yield desirable properties when incorporated into natural helical proteins. Because protein-protein interactions involving helical domains determine specificity for important biological processes such as transcriptional control, cellular differentiation, and replication, their selective disruption should be an excellent therapeutic strategy. Our results represent the first examples of the “isosteric” substitution of entire heptad repeats in α-helical coiled coil motifs in which the native global conformation is retained (Rezaei Araghi, Beilstein J. Org. Chem., 2012; Rezaei Araghi, Amino Acids, 2011; Rezaei Araghi, ChemBioChem, 2010).