A fibronectin mimetic motif improves integrin mediated cell biding to recombinant spider silk matrices.

Autor: Widhe M; Division of Protein Technology, School of Biotechnology, KTH Royal Institute of Technology, SE-106 91 Stockholm, Sweden., Shalaly ND; Division of Protein Technology, School of Biotechnology, KTH Royal Institute of Technology, SE-106 91 Stockholm, Sweden., Hedhammar M; Division of Protein Technology, School of Biotechnology, KTH Royal Institute of Technology, SE-106 91 Stockholm, Sweden; Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, SE-750 07 Uppsala, Sweden. Electronic address: my.hedhammar@slu.se.
Jazyk: angličtina
Zdroj: Biomaterials [Biomaterials] 2016 Jan; Vol. 74, pp. 256-66. Date of Electronic Publication: 2015 Oct 09.
DOI: 10.1016/j.biomaterials.2015.10.013
Abstrakt: The cell binding motif RGD is the most widely used peptide to improve cell binding properties of various biomaterials, including recombinant spider silk. In this paper we use genetic engineering to further enhance the cell supportive capacity of spider silk by presenting the RGD motif as a turn loop, similar to the one found in fibronectin (FN), but in the silk stabilized by cysteines, and therefore denoted FNCC. Human primary cells cultured on FNCC-silk showed increased attachment, spreading, stress fiber formation and focal adhesions, not only compared to RGD-silk, but also to silk fused with linear controls of the RGD containing motif from fibronectin. Cell binding to FNCC-silk was shown to involve the α5β1 integrin, and to support proliferation and migration of keratinocytes. The FNCC-silk protein allowed efficient assembly, and could even be transformed into free standing films, on which keratinocytes could readily form a monolayer culture. The results hold promise for future applications within tissue engineering.
(Copyright © 2015 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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