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

Abstract

Secondary structural conformation of hybrid oligo-peptides comprised of 1 : 1 alternating Nucleoside Derived beta-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.