The collagens are the most abundant protein family in vertebrates and a major constituent of connective tissue. Collagenous tissues like bone, cartilage, tendon, ligament, and skin meet a wide range of biomechanical requirements, such as stiffness, toughness, elasticity, and energy dissipation. This remarkable variety of mechanical properties in collagen-based tissues results from a tissue-specific hierarchical structure, ranging from the molecular conformation of the collagen molecules and their supramolecular arrangement within collagen fibrils to the morphology of the tissue itself.

Gaining detailed knowledge about the mechanical nanostructure of collagen fibrils in human ligaments is expected to reveal the links between the molecular structure of collagen fibrils and the mechanical properties of an ensemble of collagen fibrils within the ligament tissue. Anke and her team investigate whether differences in the mechanical properties of ligaments and other collagenous tissues are associated with differences in the collagen crosslink concentration.

Publications

Spitzner EC, Röper S, Zerson M, Bernstein A, Magerle R. Nanoscale Swelling Heterogeneities in Type I Collagen Fibrils. ACS Nano. 2015 Jun 23;9(6):5683-94

Dietz C, Röper S, Scherdel S, Bernstein A, Rehse N, Magerle R. Automatization of nanotomography. Rev Sci Instrum. 2007 May;78(5):053703