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Plowright R, Dinjaski N, Zhou S, et al. Influence of silk-silica fusion protein design on silica condensation . RSC Adv. 2016;6(26):21776-21788doi: 10.1039/C6RA03706B.
Plowright, R., Dinjaski, N., Zhou, S., Belton, D. J., Kaplan, D. L., & Perry, C. C. (2016). Influence of silk-silica fusion protein design on silica condensation . RSC advances, 6(26), 21776-21788. https://doi.org/10.1039/C6RA03706B
Plowright, Robyn, et al. "Influence of silk-silica fusion protein design on silica condensation ." RSC advances vol. 6,26 (2016): 21776-21788. doi: https://doi.org/10.1039/C6RA03706B
Plowright R, Dinjaski N, Zhou S, Belton DJ, Kaplan DL, Perry CC. Influence of silk-silica fusion protein design on silica condensation . RSC Adv. 2016 Jan 01;6(26):21776-21788. doi: 10.1039/C6RA03706B. Epub 2016 Feb 17. PMID: 26989487; PMCID: PMC4792305.
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RSC Adv. 2016 Jan 01;6(26):21776-21788. doi: 10.1039/C6RA03706B. Epub 2016 Feb 17.

Influence of silk-silica fusion protein design on silica condensation .

RSC advances

Robyn Plowright, Nina Dinjaski, Shun Zhou, David J Belton, David L Kaplan, Carole C Perry

Affiliations

  1. Biomolecular and Materials Interface Research Group, Interdisciplinary Biomedical Research Centre, School of Science and Technology, Nottingham Trent University, Clifton Lane, Nottingham, UK NG11 8NS.
  2. Department of Biomedical Engineering, Tufts University, 4 Colby Street, Medford, Massachusetts, 02155, United States.

PMID: 26989487 PMCID: PMC4792305 DOI: 10.1039/C6RA03706B

Abstract

Biomaterial design via genetic engineering can be utilized for the rational functionalization of proteins to promote biomaterial integration and tissue regeneration. Spider silk has been extensively studied for its biocompatibility, biodegradability and extraordinary material properties. As a protein-based biomaterial, recombinant DNA derived derivatives of spider silks have been modified with biomineralization domains which lead to silica deposition and potentially accelerated bone regeneration. However, the influence of the location of the R5 (SSKKSGSYSGSKGSKRRIL) silicifying domain fused with the spider silk protein sequence on the biosilicification process remains to be determined. Here we designed two silk-R5 fusion proteins that differed in the location of the R5 peptide, C-

Keywords: biomaterials; biomineralization; fusion proteins; silaffin; spider silk

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