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Strong, functional, tunable, self-assembling hydrogel scaffolds for regenerative medicine

Final Report Summary - STROFUNSCAFF (Strong, functional, tunable, self-assembling hydrogel scaffolds for regenerative medicine)

The project aimed to develop a new class of self-assembling bioactive hydrogel materials for regenerative medicine by integrating and taking advantage of both peptides and proteins. In addition, the project looked to enhance the complexity and functionality of these materials by working at the interface of chemistry, biology, and engineering. Through this approach, we developed a number of new material platforms (exe. 4 patents or patent applications) that enable the design and engineering of a spectrum of hydrogel materials with innovative properties that would benefit the fields of tissue engineering and regenerative properties. These platforms include a) the co-assembly of peptide amphiphiles with proteins and polysaccharides utilizing both non-covalent and covalent interactions, b) the co-assembly of peptide amphiphiles with particles such as graphene oxide, c) a co-assembling system based on peptides and disordered proteins that enable access to non-equilibrium in a controlled manner, d) a protein-based platfrom that takes advantage of ordered and disordered synergies to nucleate and guide the growth of apatite nanocrystals in a hierarchical manner and into macroscopic materials, e) novel self-assembling bioinks, and f) novel hydrogel patterning techniques. These platforms were tested towards the regeneration of tissues such as cartilage, bone, and enamel as well as to build biologically relevant in vitro models of biological scenarios such as vascular tissue, the blood-brain-barrier, and cancer. We have developed a unique set of skills that integrated supramolecular chemistry and engineering to build complex, hierarchical, and functional environments with biomolecules. The project has developed a new way to grow mineralised materials that could regenerate hard tissues such as dental enamel and bone. In addition, the study also provides insights into the role of protein disorder in human physiology and pathology

Project information

Grant agreement ID: 306873


Closed project

  • Start date

    1 August 2013

  • End date

    31 July 2018

Funded under:


  • Overall budget:

    € 1 492 686

  • EU contribution

    € 1 492 686

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