Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Self-Assembly of Recombinant Silk as a Strategy for Chemical-Free Formation of Bioactive Coatings: A Real-Time Study
KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.
KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.
KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.
Show others and affiliations
2017 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 18, no 3, p. 846-854Article in journal (Refereed) Published
Abstract [en]

Functionalization of biomaterials with biologically active peptides can improve their performance after implantation. By genetic fusion to self-assembling proteins, the functional peptides can easily be presented on different physical formats. Herein, a chemical-free coating method based on self-assembly of the recombinant spider silk protein 4RepCT is described and used to prepare functional coatings on various biomaterial surfaces. The silk assembly was studied in real-time, revealing the occurrence of continuous assembly of silk proteins onto surfaces and the formation of nanofibrillar structures. The adsorbed amounts and viscoelastic properties were evaluated, and the coatings were shown to be stable against wash with hydrogen chloride, sodium hydroxide, and ethanol. Titanium, stainless steel, and hydroxyapatite were coated with silk fused to an antimicrobial peptide or a motif from fibronectin. Human primary cells cultured on the functional silk coatings show good cell viability and proliferation, implying the potential to improve implant performance and acceptance by the body.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2017. Vol. 18, no 3, p. 846-854
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-205496DOI: 10.1021/acs.biomac.6b01721ISI: 000396379600019PubMedID: 28192654Scopus ID: 2-s2.0-85015235457OAI: oai:DiVA.org:kth-205496DiVA, id: diva2:1098510
Note

QC 20170524

Available from: 2017-05-24 Created: 2017-05-24 Last updated: 2017-11-13Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMedScopus

Authority records BETA

Hedhammar, My

Search in DiVA

By author/editor
Nilebäck, LinneaWidhe, MonaFloderus, Lotta S.Hedhammar, My
By organisation
Albanova VinnExcellence Center for Protein Technology, ProNovaProtein TechnologyCentre for Bioprocess Technology, CBioPT
In the same journal
Biomacromolecules
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 0 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf