Novel helical foldamers: organized heterogeneous backbone folding in 1 : 1 α/nucleoside-derived-β-amino acid sequencesThe work has been dedicated to Dr J. S. Yadav on his 60th birthday.Electronic supplementary information (ESI) available: Synthesis, NMR Experimental, MD and DFT data. See DOI: 10.1039/c0cc01724h

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. The backbone in hybrid oligo-peptides comprised of 1 : 1 alternating Nucleoside Derived β-Amino acid (NDA) and l -amino acid residues adopts a novel 11/8-helical fold.