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Macroscopic fibers self-assembled from recombinant miniature spider silk proteins
Department of Anatomy, Physiology, and Biochemistry, The Biomedical Centre, Swedish University of Agricultural Sciences, SE-751 23 Uppsala, Sweden.ORCID iD: 0000-0003-0140-419X
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2007 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 8, no 5, p. 1695-1701Article in journal (Refereed) Published
Abstract [en]

Strength, elasticity, and biocompatibility make spider silk an attractive resource for the production of artificial biomaterials. Spider silk proteins, spidroins, contain hundreds of repeated poly alanine/glycine-rich blocks and are difficult to produce recombinantly in soluble form. Most previous attempts to produce artificial spider silk fibers have included solubilization steps in nonphysiological solvents. It is here demonstrated that a miniature spidroin from a protein in dragline silk of Euprosthenops australis can be produced in a soluble form in Escherichia coli when fused to a highly soluble protein partner. Although this miniature spidroin contains only four poly alanine/glycine-rich blocks followed by a C-terminal non-repetitive domain, meter-long fibers are spontaneously formed after proteolytic release of the fusion partner. The structure of the fibers is similar to that of dragline silks, and although self-assembled from recombinant proteins they are as strong as fibers spun from redissolved silk. Moreover, the fibers appear to be biocompatible because human tissue culture cells can grow on and attach to the fibers. These findings enable controlled production of high-performance biofibers at large scale under physiological conditions.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2007. Vol. 8, no 5, p. 1695-1701
Keywords [en]
Animals, Arachnida/genetics/metabolism, Biocompatible Materials/chemistry/*metabolism, Escherichia coli/genetics, Fibroins/*biosynthesis/genetics/*ultrastructure, Molecular Sequence Data, Recombinant Proteins/*biosynthesis/chemistry/*ultrastructure, Solubility, Tensile Strength
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Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-250633DOI: 10.1021/bm070049yISI: 000246413600041PubMedID: 17402782Scopus ID: 2-s2.0-34249889559ISBN: 1525-7797 (Print) 1525-7797 (Linking) OAI: oai:DiVA.org:kth-250633DiVA, id: diva2:1310594
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QC 20190617

Available from: 2019-04-30 Created: 2019-04-30 Last updated: 2019-06-17Bibliographically approved

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