Computational design of a self-assembling ß-peptide oligomer.

The first computationally designed self-assembling oligomer consisting of exclusively ß-amino acids (ßAAs) is presented. The packing of a ß-3(14) helix into coiled-coils of varying stoichiometries as a function of amino acid sequence is examined. ß-Peptides with hVal repeating every third residue in the sequence appeared to have a strong propensity to pack into hexameric bundles. The designed sequence was synthesized and characterized with CD spectroscopy, NMR, and analytical ultracentrifugation, suggesting that the peptide adopts a well-folded hexameric structure.