Transformation of the structure of collagen. A time-resolved analysis of mechanochemical processes using synchrotron radiation.
Mechanochemically induced molecular transformations of collagen fibres were analysed using time-resolved small-angle diffraction spectra and histomechanical measurements. In particular, the influence of aqueous and methanolic perchlorate solutions was examined. According to a transformation continuing from the periphery towards the centre, the macroscopic contraction that is completed less than five minutes after incubation with perchlorate is caused by peripherally transformed fibrils only, whereas the centrally situated fibrils first undergo an accordion-like folding, but after more than 20 minutes are transformed similarly. The triple-helical transformation is preceded by a structure-breaking effect on structural water that can be monitored in time-resolved diffraction spectra. The combined loss of meridional low-angle reflections and cross-striated fibrils in micrographs is irreversible. By dialysis of colloidally dissolved collagen against a solution of ATP, however, segment-long spacing aggregates are obtained. Under isometric conditions, an instantaneous transformation of intermittent regions leads to an increase in the long period of adjacent, still structured regions of the same fibril that is correlated with a delayed increase in tension in the fibre. Increase of tension under isometric conditions as well as the flow-properties of a fibre relaxed in perchlorate are interpreted in terms of the parallel sliding of subunits of varying lengths, which has been demonstrated by diffraction analysis.
D000818:Animals; D003094:Collagen; D008854:Microscopy, Electron; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D051381:Rats; D013997:Time Factors; D014961:X-Ray Diffraction
D003094:Collagen