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Hindrik Mulder

Hindrik Mulder

Principal investigator

Hindrik Mulder

Fracture Mechanics of Collagen Fibrils: Influence of Natural Cross-Links

Author

  • Rene B. Svensson
  • Hindrik Mulder
  • Vuokko Kovanen
  • S. Peter Magnusson

Summary, in English

Tendons are important load-bearing structures, which are frequently injured in both sports and work. Type I collagen fibrils are the primary components of tendons and carry most of the mechanical loads experienced by the tissue, however, knowledge of how load is transmitted between and within fibrils is limited. The presence of covalent enzymatic cross-links between collagen molecules is an important factor that has been shown to influence mechanical behavior of the tendons. To improve our understanding of how molecular bonds translate into tendon mechanics, we used an atomic force microscopy technique to measure the mechanical behavior of individual collagen fibrils loaded to failure. Fibrils from human patellar tendons, rat-tail tendons (RTTs), NaBH4 reduced RTTs, and tail tendons of Zucker diabetic fat rats were tested. We found a characteristic three-phase stress-strain behavior in the human collagen fibrils. There was an initial rise in modulus followed by a plateau with reduced modulus, which was finally followed by an even greater increase in stress and modulus before failure. The RTTs also displayed the initial increase and plateau phase, but the third region was virtually absent and the plateau continued until failure. The importance of cross-link lability was investigated by NaBH4 reduction of the rat-tail fibrils, which did not alter their behavior. These findings shed light on the function of cross-links at the fibril level, but further studies will be required to establish the underlying mechanisms.

Department/s

  • Diabetes - Molecular Metabolism
  • EXODIAB: Excellence of Diabetes Research in Sweden

Publishing year

2013

Language

English

Pages

2476-2484

Publication/Series

Biophysical Journal

Volume

104

Issue

11

Document type

Journal article

Publisher

Cell Press

Topic

  • Biophysics

Status

Published

Research group

  • Diabetes - Molecular Metabolism

ISBN/ISSN/Other

  • ISSN: 1542-0086