title: Supramolecular hydrogel networks formed by molecular recognition of collagen and a peptide grafted to hyaluronic acid.
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'=157Pa) in the presence of the HA-grafted peptide compared to a mixture of collagen and HA (G'=6Pa). 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.
  
  
  
  Biopolymers of the extracellular matrix (ECM) like collagen or hyaluronan are attractive starting materials for biomaterials. While in biomaterial science covalent crosslinking is often employed, in the native ECM, stabilization and macromolecular organization is primarily based on non-covalent interactions, which allows dynamic changes of the materials. Here, we show that collagen-binding peptides, derived from the small proteoglycan decorin, grafted to hyaluronic acid enable supramolecular stabilization of collagen hydrogels. These hydrogels have storage moduli more than one order of magnitude higher than mixtures of collagen and hyaluronic acid. Furthermore, the peptide supported the structural organization of collagen. Such hydrogels could be employed for a diverse range of applications in regenerative medicine. Furthermore, the rational design helps in the understanding ECM structuring.
authors.affiliation: Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies (BCRT), Helmholtz-Zentrum Geesthacht, Kantstrasse 55, 14513 Teltow, Germany; Institute of Chemistry, University of Potsdam, 14476 Potsdam-Golm, Germany. Electronic address: stefania.federico@crick.ac.uk.
authors.forename: Stefania
authors.initials: S
authors.lastname: Federico
authors.affiliation: Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies (BCRT), Helmholtz-Zentrum Geesthacht, Kantstrasse 55, 14513 Teltow, Germany. Electronic address: ulrich.noechel@hzg.de.
authors.forename: Ulrich
authors.initials: U
authors.lastname: Nöchel
authors.affiliation: Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies (BCRT), Helmholtz-Zentrum Geesthacht, Kantstrasse 55, 14513 Teltow, Germany; Institute of Chemistry, University of Potsdam, 14476 Potsdam-Golm, Germany. Electronic address: candy.loewenberg@hzg.de.
authors.forename: Candy
authors.initials: C
authors.lastname: Löwenberg
authors.affiliation: Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies (BCRT), Helmholtz-Zentrum Geesthacht, Kantstrasse 55, 14513 Teltow, Germany; Institute of Chemistry, University of Potsdam, 14476 Potsdam-Golm, Germany. Electronic address: andreas.lendlein@hzg.de.
authors.forename: Andreas
authors.initials: A
authors.lastname: Lendlein
authors.affiliation: Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies (BCRT), Helmholtz-Zentrum Geesthacht, Kantstrasse 55, 14513 Teltow, Germany; Institute of Chemistry, University of Potsdam, 14476 Potsdam-Golm, Germany. Electronic address: axel.neffe@hzg.de.
authors.forename: Axel T
authors.initials: AT
authors.lastname: Neffe
mesh_terms: D003094:Collagen / Q000737:chemistry*; D006820:Hyaluronic Acid / Q000737:chemistry*; D020100:Hydrogels / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*
chemical_list: D020100:Hydrogels; D010455:Peptides; D006820:Hyaluronic Acid; D003094:Collagen
keywords: Biopolymers; Collagen-binding peptide; Hyaluronic acid; Hydrogels; Mechanical properties