Computational Design of a Self-Assembling β-Peptide Oligomer

The first computationally designed self-assembling oligomer consisting of exclusively beta-amino acids (beta AAs) is presented. The packing of a beta-3(14) helix into coiled-coils of varying stoichiometries as a function of amino acid sequence is examined. beta-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.