Osteoinductive recombinant silk fusion proteins for bone regeneration

Dinjaski, N., Plowright, R., Zhou, S., Belton, D.J., Perry, C.C. ORCID: 0000-0003-1517-468X and Kaplan, D.L., 2017. Osteoinductive recombinant silk fusion proteins for bone regeneration. Acta Biomaterialia, 49, pp. 127-139. ISSN 1742-7061

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Abstract

Protein polymers provide a unique opportunity for tunable designs of material systems due to the genetic basis of sequence control. To address the challenge of biomineralization interfaces with protein based materials, we genetically engineered spider silks to design organic-inorganic hybrid systems. The spider silk inspired domain (SGRGGLGGQG AGAAAAAGGA GQGGYGGLGSQGT)15 served as an organic scaffold to control material stability and to allow multiple modes of processing, whereas the hydroxyapatite binding domain VTKHLNQISQSY (VTK), provided control over osteogenesis. The VTK domain was fused either to the N-, C- or both terminals of the spider silk domain to understand the effect of position on material properties and mineralization. The addition of the VTK domain to silk did not affect the physical properties of the silk recombinant constructs, but it had a critical role in the induction of biomineralization. When the VTK domain was placed on both the C- and N-termini the formation of crystalline hydroxyapatite was significantly increased. In addition, all of the recombinant proteins in film format supported the growth and proliferation of human mesenchymal stem cells (hMSCs). Importantly, the presence of the VTK domain enhanced osteoinductive properties 2 up to 3-fold compared to the control (silk alone without VTK). Therefore, silk-VTK fusion proteins have been shown suitable for mineralization and functionalization for specific biomedical applications.

Item Type: Journal article
Publication Title: Acta Biomaterialia
Creators: Dinjaski, N., Plowright, R., Zhou, S., Belton, D.J., Perry, C.C. and Kaplan, D.L.
Publisher: Elsevier
Date: February 2017
Volume: 49
ISSN: 1742-7061
Identifiers:
NumberType
10.1016/j.actbio.2016.12.002DOI
S1742706116306717Publisher Item Identifier
Divisions: Schools > School of Science and Technology
Depositing User: Jonathan Gallacher
Date Added: 19 Dec 2017 12:07
Last Modified: 20 Dec 2017 12:03
URI: http://irep.ntu.ac.uk/id/eprint/32216

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