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Time-resolved X-ray diffraction from tendon collagen during creep using synchrotron radiation.
N Sasaki1, N Shukunami, N Matsushima
1Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan. sasaki@indy.sci.hokudai.ac.jp
Journal of Biomechanics
|March 27, 1999
Summary
Collagen tissue relaxation involves molecular elongation at low stress and molecular rearrangement at higher stress. This molecular rearrangement contributes to the observed creep behavior in collagen
Area of Science:
- Biophysics
- Materials Science
- Biomaterials
Background:
- Collagenous tissues exhibit complex relaxation phenomena.
- Understanding molecular mechanisms is crucial for tissue biomechanics.
Purpose of the Study:
- To investigate the molecular basis of relaxation in collagenous tissue.
- To analyze tension-induced deformation of the collagen D-period under creep.
Main Methods:
- Time-resolved, small-angle X-ray diffraction on bovine Achilles tendon collagen.
- Creep measurements under varying tensile stress.
Main Results:
- Tension increased the D-period, with strain (epsilon D) proportional to stress.
- At higher stress (>10 MPa), molecular elongation, gap region increase, and slippage contributed to D-period strain.
- Molecular elongation dominated strain up to 8 MPa.
- Molecular rearrangement modes exhibited creep behavior in the immediate response region.
Conclusions:
- Collagen D-period deformation involves multiple molecular processes.
- Tension-induced molecular rearrangement within the D-period underlies KWW-type relaxation.
- Findings correlate with stress-relaxation modulus observations in collagenous tissues.