title: Self-Assembly of Recombinant Silk as a Strategy for Chemical-Free Formation of Bioactive Coatings: A Real-Time Study.
abstract: 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.
authors.affiliation: KTH Royal Institute of Technology , School of Biotechnology, AlbaNova University Center, SE-106 91 Stockholm, Sweden.
authors.forename: Linnea
authors.initials: L
authors.lastname: Nilebäck
authors.affiliation: SP Technical Research Institute of Technology , SP Chemistry, Materials and Surfaces, Drottning Kristinas väg 45, SE-114 86 Stockholm, Sweden.
authors.forename: Jesper
authors.initials: J
authors.lastname: Hedin
authors.affiliation: KTH Royal Institute of Technology , School of Biotechnology, AlbaNova University Center, SE-106 91 Stockholm, Sweden.
authors.forename: Mona
authors.initials: M
authors.lastname: Widhe
authors.affiliation: KTH Royal Institute of Technology , School of Biotechnology, AlbaNova University Center, SE-106 91 Stockholm, Sweden.
authors.forename: Lotta S
authors.initials: LS
authors.lastname: Floderus
authors.affiliation: SP Technical Research Institute of Technology , SP Food and Bioscience, Soft Materials Science, Box 5401, SE-402 29 Gothenburg, Sweden.
authors.forename: Annika
authors.initials: A
authors.lastname: Krona
authors.affiliation: SP Technical Research Institute of Technology , SP Chemistry, Materials and Surfaces, Drottning Kristinas väg 45, SE-114 86 Stockholm, Sweden.
authors.forename: Helena
authors.initials: H
authors.lastname: Bysell
authors.affiliation: KTH Royal Institute of Technology , School of Biotechnology, AlbaNova University Center, SE-106 91 Stockholm, Sweden.
authors.forename: My
authors.identifier: 0000-0003-0140-419X
authors.initials: M
authors.lastname: Hedhammar
mesh_terms: D000818:Animals; D000890:Anti-Infective Agents / Q000494:pharmacology; D058491:Bacterial Load; D002448:Cell Adhesion / Q000187:drug effects; D002478:Cells, Cultured; D020099:Coated Materials, Biocompatible / Q000737:chemistry*; D042783:Endothelial Cells / Q000187:drug effects / Q000378:metabolism; D006801:Humans; D011994:Recombinant Proteins / Q000737:chemistry*; D047011:Silk / Q000737:chemistry*; D013112:Spiders; D013211:Staphylococcus aureus / Q000187:drug effects
chemical_list: D000890:Anti-Infective Agents; D020099:Coated Materials, Biocompatible; D011994:Recombinant Proteins; D047011:Silk