Structural dynamic of native tendon collagen.
The dynamic behaviour of collagen fibrils is revealed by time-resolved X-ray investigations of native rat tail tendon fibres in tensile tests.
Biomedical subjects
Publications and source records attributed to W Geercken.
The dynamic behaviour of collagen fibrils is revealed by time-resolved X-ray investigations of native rat tail tendon fibres in tensile tests.
Native collagen fibers were exposed to different dynamic loads to simulate damage to tendons and ligaments relevant clinically and for sports medicine. The results suggest that the rupture of a tendon is caused at the submicroscopic fibrillar level. Not only slow or very fast elongation, but also very fast unloading of stretched fibers seems to be responsible for disseminated damage, which reduces the stability of a fiber. This damage is induced by intrafibrillar sliding processes, which occur only a few seconds before macroscopic slippage takes place. The significance of these events for the beginning and progress of repair in vivo is discussed. The conclusions are supported by simultaneous mechanical and radiological measurements, as well as by light- and electron-microscopic results.
Small-angle x-ray diffraction spectra of dermatosparactic tendon collagen show a decreased intensity of the first order reflection. We interprete this finding to be due to the N-terminal propeptide which fills the intermolecular gap region partially.
X-ray diffraction analysis of connective tissue samples, which contain type I and type III collagen shows that twisted collagen fibrils are a general principle of assembly. The occurrence of twisted fibrils in native wet Chordae tendineae, skin and Aorta is combined with a shorter axial periodicity of about 65 nm. This shorter D period is shown to be directly related to the tilt of the molecules, which have to be curved to build-up twisted fibrils.