Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties

Biophys J. 1997 Oct;73(4):2164-72. doi: 10.1016/S0006-3495(97)78247-X.


Collagen is the primary structural element in extracellular matrices. In the form of fibers it acts to transmit forces, dissipate energy, and prevent premature mechanical failure in normal tissues. Deformation of collagen fibers involves molecular stretching and slippage, fibrillar slippage, and, ultimately, defibrillation. Our laboratory has developed a process for self-assembly of macroscopic collagen fibers that have structures and mechanical properties similar to rat tail tendon fibers. The purpose of this study is to determine the effects of subfibrillar orientation and decorin incorporation on the mechanical properties of collagen fibers. Self-assembled collagen fibers were stretched 0-50% before cross-linking and then characterized by microscopy and mechanical testing. Results of these studies indicate that fibrillar orientation, packing, and ultimate tensile strength can be increased by stretching. In addition, it is shown that decorin incorporation increases ultimate tensile strength of uncross-linked fibers. Based on the observed results it is hypothesized that decorin facilitates fibrillar slippage during deformation and thereby improves the tensile properties of collagen fibers.

MeSH terms

  • Animals
  • Biomechanical Phenomena
  • Biophysical Phenomena
  • Biophysics
  • Collagen / chemistry*
  • Collagen / physiology*
  • Collagen / ultrastructure
  • Cross-Linking Reagents
  • Decorin
  • Extracellular Matrix Proteins
  • In Vitro Techniques
  • Macromolecular Substances
  • Microscopy, Electron
  • Protein Conformation
  • Proteoglycans / chemistry*
  • Proteoglycans / physiology*
  • Proteoglycans / ultrastructure
  • Rats
  • Rats, Sprague-Dawley
  • Tendons / chemistry
  • Tensile Strength
  • Uronic Acids


  • Cross-Linking Reagents
  • Dcn protein, rat
  • Decorin
  • Extracellular Matrix Proteins
  • Macromolecular Substances
  • Proteoglycans
  • Uronic Acids
  • Collagen