Abstract
Reconstituted type I collagen fibres have received considerable interest as tendon implant materials due to their chemical and structural similarity to the native tissue. Fibres produced through a semi-continuous extrusion process were cross-linked with different concentrations of the zero-length cross-linker 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) in combination with N-hydroxysuccinimide (NHS). Tensile properties of the fibres were considered, along with imaging of both surface structure and fibrillar alignment. Resistance of the fibres to bacterial collagenase was investigated and fibre sections seeded with human tendon cells for biological characterization, including cell adhesion and proliferation. The work clearly demonstrated that whilst the concentration of EDC and NHS had no significant effect on the mechanics, a higher concentration was associated with higher collagenase resistance, but also provided a less attractive surface for cell adhesion and proliferation. A lower cross-linking concentration offered a more biocompatible material without reduction in mechanics and with a potentially more optimal degradability.
Highlights
Tendons can be considered as unidirectional fibre-reinforced composites and serve to transmit the forces generated by muscle contraction with a minimal dispersion of energy [1]
Tensile loading demonstrated that the concentration of the ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) and NHS could be reduced by 100 times from the standard cross-linking concentration without influence on the ultimate tensile strength of the fibres
Whilst the author’s previous study clearly showed EDC/NHS cross-linking to significantly increase mechanical properties of fibre constructs [41], this current study has shown that less extreme cross-linking conditions can be considered without detriment to mechanics
Summary
Tendons can be considered as unidirectional fibre-reinforced composites and serve to transmit the forces generated by muscle contraction with a minimal dispersion of energy [1]. Whilst the principal role of tendon must be to resist tension, a certain degree of compliance is necessary [1] These conflicting demands are resolved as a result of the hierarchical structure of tendon, the ‘crimped’ nature of the collagen fibres [1] and the contrasting nature of the stiff collagen and the viscous, highly hydrated and proteoglycan-rich surrounding matrix [2]. In addition to their mechanical demands, tendons must support cellular activity [3, 4]. Surgery for tendinopathy or rupture is considered a last resort and typically consists of simple repair
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