Novel helical foldamers: organized heterogeneous backbone folding in 1:1 αueleoside-derived-β-amino acid sequences

摘要

Secondary structural conformation of hybrid oligo-peptides comprised of 1:1 alternating Nucleoside Derived β-Amino acid (NDA) and L -amino acid residues has been reported. The studies reveal that the NDA residues organize the heterogeneous backbone featuring the surface properties of both nucleic acids and peptides, to adopt a novel 11/8-helical fold.rnHybrid peptides comprised of natural α and unnatural cyclic β-amino acids, particularly in 1:1, 1:2 and 2:1 ratios have emerged as new generation foldamers.