Formation of stable secondary structures by oligomers that mimic natural peptides is a key asset for enhanced biological response. β(3) -Peptides with an additional methylene group in their backbone are proteolytically stable and fold into stable 14-helical structures in solution. Here we show that oligomeric β(3) -hexapeptides synthesized from L-aspartic acid monomers (β(3) -peptides 1, 5a and 6) or homologated β(3) -amino acids (β(3) -peptide 2), fold into similar stable 14-helical secondary structures in solution, except that the former form right-handed 14-helix and the later form left-handed 14-helix. β(3) -Peptides from L-Asp monomers contain an additional amide bond in the side chains that provides opportunities for more hydrogen bonding. However based on the NMR solution structures, we found that β(3) -peptide from L-Asp monomers (1) and from homologated amino acids (2) form similar structures with no additional side chain interactions. These results suggest that the β(3) -peptides derived from L-Asp are promising peptide-mimetics that can be readily synthesized using L-Asp monomers as well as the right-handed 14-helical conformation of these β(3) -peptides (such as 1 and 6) may prove beneficial in the design of mimics for right-handed α -helix of α -peptides.