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  Dynamic mechanical control of alginate-fibronectin hydrogels with dual crosslinking : covalent and ionic

Trujillo, S., Seow, M., Lueckgen, A., Salmeron-Sanchez, M., & Cipitria, A. (2021). Dynamic mechanical control of alginate-fibronectin hydrogels with dual crosslinking: covalent and ionic. Polymers, 13(3): 433. doi:10.3390/polym13030433.

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Trujillo, Sara, Author
Seow, Melanie, Author
Lueckgen, Aline, Author
Salmeron-Sanchez, Manuel, Author
Cipitria, Amaia1, Author              
Affiliations:
1Amaia Cipitria, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2489692              

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Free keywords: alginate hydrogel; fibronectin; enzymatic degradation; dual crosslinking; covalent and ionic crosslinking; dynamic mechanical properties
 Abstract: Alginate is a polysaccharide used extensively in biomedical applications due to its biocompatibility and suitability for hydrogel fabrication using mild reaction chemistries. Though alginate has commonly been crosslinked using divalent cations, covalent crosslinking chemistries have also been developed. Hydrogels with tuneable mechanical properties are required for many biomedical applications to mimic the stiffness of different tissues. Here, we present a strategy to engineer alginate hydrogels with tuneable mechanical properties by covalent crosslinking of a norbornene-modified alginate using ultraviolet (UV)-initiated thiol-ene chemistry. We also demonstrate that the system can be functionalised with cues such as full-length fibronectin and protease-degradable sequences. Finally, we take advantage of alginate’s ability to be crosslinked covalently and ionically to design dual crosslinked constructs enabling dynamic control of mechanical properties, with gels that undergo cycles of stiffening–softening by adding and quenching calcium cations. Overall, we present a versatile hydrogel with tuneable and dynamic mechanical properties, and incorporate cell-interactive features such as cell-mediated protease-induced degradability and full-length proteins, which may find applications in a variety of biomedical contexts.

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Language(s): eng - English
 Dates: 2021-01-292021
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.3390/polym13030433
BibTex Citekey: polym13030433
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Title: Polymers
Source Genre: Journal
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Publ. Info: Basel, Switzerland : MDPI AG
Pages: - Volume / Issue: 13 (3) Sequence Number: 433 Start / End Page: - Identifier: ISSN: 2073-4360