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Enhanced recombinant protein scaffolds for bone tissue engineering

Tissue engineering is the repair of structure and function of damaged body tissues. In recent years many new materials were developed for use in tissue engineering, and especially genetically engineered proteins are very promising.

Genetically engineered proteins are inspired by natural proteins, and produced by recombinant DNA technology. The proteins we developed can self-assemble to form hydrogel scaffolds with tunable mechanical properties (Figure 1). In addition, the recombinant production technique enables easy implementation of bioactive peptides. For example, the binding peptide RGD (arginine-glycine-aspartic acid) and heparin binding domains (ex. lysine-arginine-serine-arginine (KSRS)) can greatly improve the material-cell interactions. This way, we are able to develop hydrogels composed of proteins that are functionalized to achieve better biological performance.

In this project we will study the physico-chemical properties and the biocompatibility of a new genetically engineered protein that was developed in our lab very recently. The goal is to obtain well-characterized hydrogel scaffold that can be used for biological evaluation. To this end, we will study fiber formation using AFM, hydrogel formation and mechanical properties with rheology and stability studies using light scattering and spectrophotometry. In a second stage we will analyze the affinity to calcium of the obtained scaffolds, which is an indication of the ability to mineralize. In addition, we will perform a drug release study.

Experimental techniques:

1     Atomic force microscopy (AFM)

2     Rheology

3     Dynamic light scattering (DLS)

4     Spectrophotometry

More information? Please contact Gosia Wlodarczyk-Biegun


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Sengupta, D. and S.C. Heilshorn, Protein-Engineered Biomaterials: Highly Tunable Tissue Engineering Scaffolds. Tissue Engineering Part B-Reviews, 2010. 16(3): p. 285-293.

Shin, H., et al., Biomimetic materials for tissue engineering. Biomaterials, 2003. 24: p. 4353–4364.