Nonpeptidic foldamers from amino acids: synthesis and characterization of 1,3-substituted triazole oligomers.

Nonpeptidic foldamers capable of displaying protein-like functionality were prepared by swapping amide bonds with 1,2,3-triazole rings. The overall conformation of these triazole oligomers is largely dictated by dipole-dipole interactions between adjacent rings. Solution NMR studies suggest that a zigzag conformation, which closely mimics the beta-strand structure, predominates in two different tetramers.