Multi-hierarchical self-assembly of a collagen mimetic peptide from triple helix to nanofibre and hy

Abstract

Replicating the multi-hierarchical self-assembly of collagen has long-attracted scientists, from both the perspective of the fundamental science of supramolecular chemistry and that of potential biomedical applications in tissue engineering. Many approaches to drive the self-assembly of synthetic systems through the same steps as those of natural collagen (peptide chain to triple helix to nanofibres and, finally, to a hydrogel) are partially successful, but none simultaneously demonstrate all the levels of structural assembly. Here we describe a peptide that replicates the self-assembly of collagen through each of these steps. The peptide features collagen's characteristic proline–hydroxyproline–glycine repeating unit, complemented by designed salt-bridged hydrogen bonds between lysine and aspartate to stabilize the triple helix in a sticky-ended assembly. This assembly is propagated into nanofibres with characteristic triple helical packing and lengths with a lower bound of several hundred nanometres. These nanofibres form a hydrogel that is degraded by collagenase at a similar rate to that of natural collagen. A short, synthetic peptide has been prepared that mimics much of the assembly process of natural collagen. Electrostatic interactions are used to create a sticky-ended structure, which in turn self-assembles through several levels of structural hierarchy from peptide to triple helix to nanofibre and finally to hydrogel.

Cite this article

O'Leary, L., Fallas, J., Bakota, E. et al. Multi-hierarchical self-assembly of a collagen mimetic peptide from triple helix to nanofibre and hydrogel. Nature Chem 3, 821–828 (2011). https://doi.org/10.1038/nchem.1123

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