@misc{federico_supramolecular_hydrogel_2016, 
author={Federico, S.,Noechel, U.,Loewenberg, C.,Lendlein, A.,Neffe, A.T.},
title={Supramolecular hydrogel networks formed by molecular recognition of collagen and a peptide grafted to hyaluronic acid},
year={2016},
howpublished = {journal article},
doi = {https://doi.org/10.1016/j.actbio.2016.04.018},
abstract = {The extracellular matrix (ECM) is a nano-structured, highly complex hydrogel, in which the macromolecules are organized primarily by non-covalent interactions. Here, in a biomimetic approach, the decorin-derived collagen-binding peptide LSELRLHNN was grafted to hyaluronic acid (HA) in order to enable the formation of a supramolecular hydrogel network together with collagen. The storage modulus of a mixture of collagen and HA was increased by more than one order of magnitude (G′ = 157 Pa) in the presence of the HA-grafted peptide compared to a mixture of collagen and HA (G′ = 6 Pa). The collagen fibril diameter was decreased, as quantified using electron microscopy, in the presence of the HA-grafted peptide. Here, the peptide mimicked the function of decorin by spatially organizing collagen. The advantage of this approach is that the non-covalent crosslinks between collagen molecules and the HA chains created by the peptide form a reversible and dynamic hydrogel, which could be employed for a diverse range of applications in regenerative medicine.},
note = {Online available at: \url{https://doi.org/10.1016/j.actbio.2016.04.018} (DOI). Federico, S.; Noechel, U.; Loewenberg, C.; Lendlein, A.; Neffe, A.: Supramolecular hydrogel networks formed by molecular recognition of collagen and a peptide grafted to hyaluronic acid. Acta Biomaterialia. 2016. vol. 38, 1-10. DOI: 10.1016/j.actbio.2016.04.018}}