| Autor: |
O'Leary LE; Departments of Chemistry and Bioengineering Rice University, Houston, Texas 77005, USA., Fallas JA, Bakota EL, Kang MK, Hartgerink JD |
| Jazyk: |
angličtina |
| Zdroj: |
Nature chemistry [Nat Chem] 2011 Aug 28; Vol. 3 (10), pp. 821-8. Date of Electronic Publication: 2011 Aug 28. |
| DOI: |
10.1038/nchem.1123 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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