Abstract
The hierarchical assembly of collagen-based triple helical peptides into disks, followed by metal-promoted assembly into microcages is described. The length of the triple helix was found to correlate to the height of the disks that formed, providing mechanistic insights into their formation. The encapsulation of fluorescently labeled dextrans within the peptide microcages, and their subsequent thermal release is detailed. The half-life for thermal release of the encapsulated cargo from the cages was found to increase as the peptide triple helix stability increased, providing a means to engineer cargo delivery rates through peptide design.
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