A collagen peptide was designed for metal-triggered, hierarchical assembly through a radial growth mechanism. To achieve radial assembly, H-(byp)(2) containing Pro-Hyp-Gly repeating sequences and two staggered bipyridine ligands within the peptide was synthesized. Triple helix formation resulted in the placement of six bipyridine ligands along the triple helix, and the addition of metal ions resulted in the formation of nanometer-sized collagen peptide disks. These structures were found to disassemble upon the addition of EDTA, demonstrating that radial assembly of collagen peptide triple helices could be realized with the addition of metal ions.