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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.

SUBMITTER: Jacobsen MM

PROVIDER: S-EPMC5381220 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

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Silk-fibronectin protein alloy fibres support cell adhesion and viability as a high strength, matrix fibre analogue.

Jacobsen Matthew M MM Li David D Gyune Rim Nae N Backman Daniel D Smith Michael L ML Wong Joyce Y JY

Scientific reports 20170405

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 sp ...[more]

PMID: 28378749

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Project description:The cell-dependent polymerization of intercellular fibronectin fibrils can stimulate cells to self-assemble into multicellular structures. The local physical cues that support fibronectin-mediated cellular self-assembly are largely unknown. Here, fibronectin matrix analogs were used as synthetic adhesive substrates to model cell-matrix fibronectin fibrils having different integrin-binding specificity, affinity, and/or density. We utilized this model to quantitatively assess the relationship between adhesive forces derived from cell-substrate interactions and the ability of fibronectin fibril assembly to induce cellular self-assembly. Results indicate that the strength of initial, rather than mature, cell-substrate attachments correlates with the ability of substrates to support fibronectin-mediated cellular self-assembly. The cellular response to soluble fibronectin was bimodal and independent of the integrin-binding specificity of the substrate; increasing soluble fibronectin levels above a critical threshold increased aggregate cohesion on permissive substrates. Once aggregates formed, continuous fibronectin polymerization was necessary to maintain cohesion. During self-assembly, soluble fibronectin decreased cell-substrate adhesion strength and induced aggregate cohesion via a Rho-dependent mechanism, suggesting that the balance of contractile forces derived from fibronectin fibrils within cell-cell versus cell-substrate adhesions controls self-assembly and aggregate cohesion. Thus, initial cell-substrate attachment strength may provide a quantitative basis with which to build predictive models of fibronectin-mediated microtissue fabrication on a variety of substrates.Statement of significanceCellular self-assembly is a process by which cells and extracellular matrix (ECM) proteins spontaneously organize into three-dimensional (3D) tissues in the absence of external forces. Cellular self-assembly can be initiated in vitro, and represents a potential tool for tissue engineers to organize cells into modular building blocks for artificial tissue fabrication. Fibronectin is an ECM protein that plays a key role in tissue formation during embryonic development. Additionally, the cell-mediated process of converting soluble fibronectin into insoluble, ECM-associated fibrils has been shown to initiate cellular self-assembly in vitro. In this study, we examine the relationship between the strength of cell-substrate adhesions and the ability of fibronectin fibril assembly to induce cellular self-assembly. Our results indicate that substrate composition and density play cooperative roles with cell-mediated fibronectin matrix assembly to control the transition of cells from 2D monolayers into 3D multicellular aggregates. Results of this study provide a quantitative approach to build predictive models of cellular self-assembly, as well as a simple cell-culture platform to produce biomimetic units for modular tissue engineering.

Dataset Information

Silk-fibronectin protein alloy fibres support cell adhesion and viability as a high strength, matrix fibre analogue.

Publications

Silk-fibronectin protein alloy fibres support cell adhesion and viability as a high strength, matrix fibre analogue.

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