Fibrillar structure and mechanical properties of collagen.
Collagen type I is among the most important stress-carrying protein structures in mammals. Despite their importance for the outstanding mechanical properties of this tissue, there is still a lack of understanding of the processes that lead to the specific shape of the stress-strain curve of collagen. Recent in situ synchrotron X-ray scattering experiments suggest that several different processes could dominate depending on the amount of strain. While at small strains there is a straightening of kinks in the collagen structure, first at the fibrillar then at the molecular level, higher strains lead to molecular gliding within the fibrils and ultimately to a disruption of the fibril structure. Moreover, it was observed that the strain within collagen fibrils is always considerably smaller than in the whole tendon. This phenomenon is still very poorly understood but points toward the existence of additional gliding processes occurring at the interfibrillar level.
Materials Physics Institute and Ludwig-Boltzmann Institute of Osteology, University of Wien, Strudlhofgasse 4, Wien, A-1090, Austria. fratzl@unileoben.ac.at
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D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000502:physiology*; D018360:Crystallography, X-Ray; D006801:Humans; D013314:Stress, Mechanical; D013329:Structure-Activity Relationship
D003094:Collagen