Helical Sense Control of Metal–Peptide Torus Frameworks Leading to the Folding and Assembly of a Ag<sub>21</sub>L<sub>14</sub> Braided Peptide Nanotube
Sota Oguma, Yuuki Inomata, Akihiro Hayakawa, Takahiro Nakama, Makoto Fujita, Tomohisa Sawada
Abstract
High Resolution Image Download MS PowerPoint Slide The chirality of helical polypeptides is correlated to that of their constituent amino acid residues. For polypeptides with non-natural backbones, however, such correlations are less clear. Here, circular double helices with torus knot/link topologies were assembled from non-natural metal–peptide chains composed of Ag(I) ions and ditopic tripeptides with Gly-Gly-Ala and Gly-Ala-Gly sequences. We found that the chirality of the assembled helical structures is determined by the l -Ala’s dihedral angles. A tubular dimeric structure with an M 21 L 14 composition was further achieved via additional metal cross-linking, showing rational design potential for artificial peptide helices.