title: Viscoelastic properties of collagen: synchrotron radiation investigations and structural model.
abstract: Collagen type I is the most abundant structural protein in tendon, skin and bone, and largely determines the mechanical behaviour of these connective tissues. To obtain a better understanding of the relationship between structure and mechanical properties, tensile tests and synchrotron X-ray scattering have been carried out simultaneously, correlating the mechanical behaviour with changes in the microstructure. Because intermolecular cross-links are thought to have a great influence on the mechanical behaviour of collagen, we also carried out experiments using cross-link-deficient tail-tendon collagen from rats fed with beta-APN, in addition to normal controls. The load-elongation curve of tendon collagen has a characteristic shape with, initially, an increasing slope, corresponding to an increasing stiffness, followed by yielding and then fracture. Cross-link-deficient collagen produces a quite different curve with a marked plateau appearing in some cases, where the length of the tendon increases at constant stress. With the use of in situ X-ray diffraction, it was possible to measure simultaneously the elongation of the collagen fibrils inside the tendon and of the tendon as a whole. The overall strain of the tendon was always larger than the strain in the individual fibrils, which demonstrates that some deformation is taking place in the matrix between fibrils. Moreover, the ratio of fibril strain to tendon strain was dependent on the applied strain rate. When the speed of deformation was increased, this ratio increased in normal collagen but generally decreased in cross-link-deficient collagen, correlating to the appearance of a plateau in the force-elongation curve indicating creep. We proposed a simple structural model, which describes the tendon at a hierarchical level, where fibrils and interfibrillar matrix act as coupled viscoelastic systems. All qualitative features of the strain-rate dependence of both normal and cross-link-deficient collagen can be reproduced within this model. This complements earlier models that considered the next smallest level of hierarchy, describing the deformation of collagen fibrils in terms of changes in their molecular packing.
authors.affiliation: Erich Schmid Institute of Materials Science, Austrian Academy of Sciences, and University of Leoben, Jahnstrasse 12, 8700 Leoben, Austria.
authors.forename: R
authors.initials: R
authors.lastname: Puxkandl
authors.forename: I
authors.initials: I
authors.lastname: Zizak
authors.forename: O
authors.initials: O
authors.lastname: Paris
authors.forename: J
authors.initials: J
authors.lastname: Keckes
authors.forename: W
authors.initials: W
authors.lastname: Tesch
authors.forename: S
authors.initials: S
authors.lastname: Bernstorff
authors.forename: P
authors.initials: P
authors.lastname: Purslow
authors.forename: P
authors.initials: P
authors.lastname: Fratzl
mesh_terms: D000818:Animals; D024042:Collagen Type I / Q000737:chemistry*; D004548:Elasticity; D008958:Models, Molecular; D011487:Protein Conformation; D051381:Rats; D013314:Stress, Mechanical; D017356:Synchrotrons; D013623:Tail / Q000737:chemistry; D013710:Tendons / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D024042:Collagen Type I