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  1. Here, the hierarchical assembly of a collagen mimetic peptide (CMP) displaying four bipyridine moieties is described. The CMP was capable of forming triple helices followed by self-assembly into disks and domes. Treatment of these disks and domes with metal ions such as Fe(II), Cu(II), Zn(II), Co(II), and Ru(III) triggered the formation of microcages, and micron-sized cup-like structures. Mechanistic studies suggest that the formation of the microcages proceeds from the disks and domes in a metal-dependent fashion. Fluorescently-labeled dextrans were encapsulated within the cages and displayed a time-dependent release using thermal conditions. 
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  2. Abstract

    Metal ion‐mediated assembly of peptides is an intriguing method for developing novel biomaterials. In particular, peptide building blocks based on collagen triple helical and coiled‐coil peptides have been functionalized with metal‐binding ligands and assemble into hierarchical structures with diverse potential applications. This review outlines the use of metal‐mediated assembly with these supramolecular structures and highlights how changes in the building blocks lead to significant differences in structural morphologies, with the identity of the metal‐binding ligands and their placement on the building block as crucial aspects in the bottom‐up development of the assemblies.

     
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