Osmotic pressure induced tensile forces in tendon collagen

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...

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Bibliographic Details
Published in:Nature communications 2015-01, Vol.6 (1), p.5942-5942, Article 5942
Main Authors: Masic, Admir, Bertinetti, Luca, Schuetz, Roman, Chang, Shu-Wei, Metzger, Till Hartmut, Buehler, Markus J., Fratzl, Peter
Format: Article
Language:English
Subjects:
119/118
140/133
639/301/54
Animals
Bone and Bones - pathology
Collagen - chemistry
Female
Humanities and Social Sciences
Molecular Dynamics Simulation
multidisciplinary
Muscle Contraction
Osmosis
Osmotic Pressure
Pressure
Rats
Rats, Sprague-Dawley
Scattering, Radiation
Science
Science (multidisciplinary)
Spectrum Analysis, Raman
Stress, Mechanical
Temperature
Tendons - pathology
Tensile Strength
Water - chemistry
X-Ray Diffraction
X-Rays
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Summary: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. Water is an important component of collagen in tendons, bone and extracellular matrix, but its role in the mechanical function of protein is poorly understood. Here, the authors study the effects of osmotic pressure on contraction in collagen, suggesting that collagen could function as a mechanical actuator.
ISSN:2041-1723
2041-1723
DOI:10.1038/ncomms6942