Abstract
Formation of stable secondary structures by alogimers that minic nutral pepitdes is a key asset for nhanced biological reponse. Here we show that aligomerie beta(3)-hexapeptides synthesized from L-aspartic acid monomers (beta(3)-peptides 1, 5a, and 6) or homologated beta(3)-amino acids (beta(3)-peptide 2), fold into smilar stable 14-hedical secondary strures in soludtion except that the former left-handed 14-helix. beta(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 I\IMR solution structures, we found that beta(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 beta(3)-peptides derived from L-Asp are promising peptide-mimetics that can he readily synthesized using L-Asp monomers as well as the right-handed 14-helical conformation of these beta(3)-peptides (such as 1 and 6) may prove benefical in the design of animal for right-handed alpha-helix f alpha-peptides (C) 2014 Wiley periodicals Inc.