Crosslinking of discrete self-assembled collagen threads: Effects on mechanical strength and cell-matrix interactions

J Biomed Mater Res A. 2007 Feb;80(2):362-71. doi: 10.1002/jbm.a.30893.

Abstract

Bundles of threads extruded from type I collagen have been researched extensively as scaffolds to promote the repair and regeneration of torn tendons and ligaments. The success of these scaffolds has been limited by insufficient tissue ingrowth from the wound margin, which may be inhibited by the chemical or physical crosslinking treatment used to increase the mechanical properties and decrease the degradation rate of these scaffolds. Recently, self-assembled collagen threads extruded from solutions of type I collagen molecules were shown to possess ultimate tensile strengths and structural properties comparable to native tendon fibers; however the tissue response to these threads has yet to be determined. The goal of this study was to investigate the effects of various crosslinking techniques on the mechanical properties as well as the in vitro rate of new tissue ingrowth on these threads. Our findings indicate that the physical crosslinking techniques, dehydrothermal (DHT) or ultraviolet light (UV), most significantly improve the mechanical strengths of the threads, but most significantly decrease the rate of cell migration. In contrast, carbodiimide (EDC) crosslinking achieved sub-optimal strength generation, but demonstrated improved cell migration rates. Future studies will investigate the design of threads with surface biochemistries that maximize tissue ingrowth while maintaining the mechanical stability of the scaffold.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Cell Movement / drug effects*
  • Cells, Cultured
  • Collagen Type I / chemistry*
  • Cross-Linking Reagents
  • Ligaments
  • Mechanics
  • Rats
  • Rats, Sprague-Dawley
  • Regeneration / drug effects
  • Tendons
  • Tissue Engineering / methods*
  • Ultraviolet Rays
  • Wound Healing / drug effects*

Substances

  • Collagen Type I
  • Cross-Linking Reagents