Change search
ReferencesLink to record
Permanent link

Direct link
Recombinant Spider Silk Genetically Functionalized with Affinity Domains
Show others and affiliations
2014 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 15, no 5, 1696-1706 p.Article in journal (Refereed) Published
Abstract [en]

Functionalization of biocompatible materials for presentation of active protein domains is an area of growing interest. Herein, we describe a strategy for functionalization of recombinant spider silk via gene fusion to affinity domains of broad biotechnological use. Four affinity domains of different origin and structure; the IgG-binding domains Z and C2, the albumin-binding domain ABD, and the biotin-binding domain M4, were all successfully produced as soluble silk fusion proteins under nondenaturing purification conditions. Silk films and fibers produced from the fusion proteins were demonstrated to be chemically and thermally stable. Still, the bioactive domains are concluded to be folded and accessible, since their respective targets could be selectively captured from complex samples, including rabbit serum and human plasma. Interestingly, materials produced from mixtures of two different silk fusion proteins displayed combined binding properties, suggesting that tailor-made materials with desired stoichiometry and surface distributions of several binding domains can be produced. Further, use of the IgG binding ability as a general mean for presentation of desired biomolecules could be demonstrated for a human vascular endothelial growth factor (hVEGF) model system, via a first capture of anti-VEGF IgG to silk containing the Z-domain, followed by incubation with hVEGF. Taken together, this study demonstrates the potential of recombinant silk, genetically functionalized with affinity domains, for construction of biomaterials capable of presentation of almost any desired biomolecule.

Place, publisher, year, edition, pages
2014. Vol. 15, no 5, 1696-1706 p.
Keyword [en]
Streptococcal Protein-G, Binding-Proteins, Fusion Proteins, Serum-Albumin, Fibroin, Cell, Fibers, Biomaterials, Antibody, Bundle
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:kth:diva-146554DOI: 10.1021/bm500114eISI: 000335939800016ScopusID: 2-s2.0-84900422237OAI: diva2:724246
Swedish Research CouncilVinnova

QC 20140612

Available from: 2014-06-12 Created: 2014-06-12 Last updated: 2014-06-12Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textScopus

Search in DiVA

By author/editor
Nygren, Per-Åke
By organisation
Protein Technology
In the same journal
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 71 hits
ReferencesLink to record
Permanent link

Direct link