Osmotic pressure induced tensile forces in tendon collagen

Publikation: Beitrag in FachzeitschriftForschungsartikelBeigetragenBegutachtung

Beitragende

  • Admir Masic - , Max Planck Institute of Colloids and Interfaces (Autor:in)
  • Luca Bertinetti - , Max Planck Institute of Colloids and Interfaces (Autor:in)
  • Roman Schuetz - , Max Planck Institute of Colloids and Interfaces (Autor:in)
  • Shu Wei Chang - , Massachusetts Institute of Technology (MIT) (Autor:in)
  • Till Hartmut Metzger - , Max Planck Institute of Colloids and Interfaces (Autor:in)
  • Markus J. Buehler - , Massachusetts Institute of Technology (MIT) (Autor:in)
  • Peter Fratzl - , Max Planck Institute of Colloids and Interfaces (Autor:in)

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.

Details

OriginalspracheEnglisch
Aufsatznummer5942
FachzeitschriftNature communications
Jahrgang6
PublikationsstatusVeröffentlicht - 22 Jan. 2015
Peer-Review-StatusJa
Extern publiziertJa

Externe IDs

PubMed 25608644
ORCID /0000-0002-4666-9610/work/142238931