title: Silk-fibronectin protein alloy fibres support cell adhesion and viability as a high strength, matrix fibre analogue.
abstract: Silk is a natural polymer with broad utility in biomedical applications because it exhibits general biocompatibility and high tensile material properties. While mechanical integrity is important for most biomaterial applications, proper function and integration also requires biomaterial incorporation into complex surrounding tissues for many physiologically relevant processes such as wound healing. In this study, we spin silk fibroin into a protein alloy fibre with whole fibronectin using wet spinning approaches in order to synergize their respective strength and cell interaction capabilities. Results demonstrate that silk fibroin alone is a poor adhesive surface for fibroblasts, endothelial cells, and vascular smooth muscle cells in the absence of serum. However, significantly improved cell attachment is observed to silk-fibronectin alloy fibres without serum present while not compromising the fibres' mechanical integrity. Additionally, cell viability is improved up to six fold on alloy fibres when serum is present while migration and spreading generally increase as well. These findings demonstrate the utility of composite protein alloys as inexpensive and effective means to create durable, biologically active biomaterials.
authors.affiliation: Department of Biomedical Engineering, Boston University, 44 Cummington Mall, Boston, 02215, Massachusetts, USA.
authors.forename: Matthew M
authors.initials: MM
authors.lastname: Jacobsen
authors.affiliation: Department of Biomedical Engineering, Boston University, 44 Cummington Mall, Boston, 02215, Massachusetts, USA.
authors.forename: David
authors.initials: D
authors.lastname: Li
authors.affiliation: Department of Biomedical Engineering, Boston University, 44 Cummington Mall, Boston, 02215, Massachusetts, USA.
authors.forename: Nae
authors.initials: N
authors.lastname: Gyune Rim
authors.affiliation: Department of Biomedical Engineering, Boston University, 44 Cummington Mall, Boston, 02215, Massachusetts, USA.
authors.forename: Daniel
authors.initials: D
authors.lastname: Backman
authors.affiliation: Department of Biomedical Engineering, Boston University, 44 Cummington Mall, Boston, 02215, Massachusetts, USA.
authors.forename: Michael L
authors.initials: ML
authors.lastname: Smith
authors.affiliation: Department of Biomedical Engineering, Boston University, 44 Cummington Mall, Boston, 02215, Massachusetts, USA.
authors.forename: Joyce Y
authors.initials: JY
authors.lastname: Wong
mesh_terms: D000818:Animals; D002417:Cattle; D002448:Cell Adhesion / Q000187:drug effects*; D002470:Cell Survival / Q000187:drug effects; D002478:Cells, Cultured; D042783:Endothelial Cells / Q000187:drug effects / Q000502:physiology; D005347:Fibroblasts / Q000187:drug effects / Q000502:physiology; D005349:Fibroins / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism*; D055595:Mechanical Phenomena; D051379:Mice; D032389:Myocytes, Smooth Muscle / Q000187:drug effects / Q000502:physiology; D014014:Tissue Adhesives / Q000378:metabolism*
chemical_list: D005353:Fibronectins; D014014:Tissue Adhesives; D005349:Fibroins