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Osmotic pressure induced tensile forces in tendon collagen

Author

Listed:
  • Admir Masic

    (Max Planck Institute for Colloids and Interfaces)

  • Luca Bertinetti

    (Max Planck Institute for Colloids and Interfaces)

  • Roman Schuetz

    (Max Planck Institute for Colloids and Interfaces)

  • Shu-Wei Chang

    (Laboratory for Atomistic and Molecular Mechanics, MIT)

  • Till Hartmut Metzger

    (Max Planck Institute for Colloids and Interfaces)

  • Markus J. Buehler

    (Laboratory for Atomistic and Molecular Mechanics, MIT)

  • Peter Fratzl

    (Max Planck Institute for Colloids and Interfaces)

Abstract

Water is an important component of collagen in tendons, but its role for the function of this load-carrying protein structure is poorly understood. Here we use a combination of multi-scale experimentation and computation to show that water is an integral part of the collagen molecule, which changes conformation upon water removal. The consequence is a shortening of the molecule that translates into tensile stresses in the range of several to almost 100 MPa, largely surpassing those of about 0.3 MPa generated by contractile muscles. Although a complete drying of collagen would be relevant for technical applications, such as the fabrication of leather or parchment, stresses comparable to muscle contraction already occur at small osmotic pressures common in biological environments. We suggest, therefore, that water-generated tensile stresses may play a role in living collagen-based materials such as tendon or bone.

Suggested Citation

  • Admir Masic & Luca Bertinetti & Roman Schuetz & Shu-Wei Chang & Till Hartmut Metzger & Markus J. Buehler & Peter Fratzl, 2015. "Osmotic pressure induced tensile forces in tendon collagen," Nature Communications, Nature, vol. 6(1), pages 1-8, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms6942
    DOI: 10.1038/ncomms6942
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    Cited by:

    1. Katrein Sauer & Ivo Zizak & Jean-Baptiste Forien & Alexander Rack & Ernesto Scoppola & Paul Zaslansky, 2022. "Primary radiation damage in bone evolves via collagen destruction by photoelectrons and secondary emission self-absorption," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Benedikt Rennekamp & Christoph Karfusehr & Markus Kurth & Aysecan Ünal & Debora Monego & Kai Riedmiller & Ganna Gryn’ova & David M. Hudson & Frauke Gräter, 2023. "Collagen breaks at weak sacrificial bonds taming its mechanoradicals," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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