Nonlinear Stress-Induced Transformations in Collagen Fibrillar Organization, Disorder and Strain Mechanisms in the Bone-Cartilage Unit.
Autor: | Badar W; Centre for Bioengineering and School of Engineering and Materials Science, Queen Mary University of London, London, E1 4NS, UK., Inamdar SR; Centre for Bioengineering and School of Engineering and Materials Science, Queen Mary University of London, London, E1 4NS, UK., Fratzl P; Max Planck Institute of Colloids and Interfaces, Research Campus Golm, 14424, Potsdam, Germany., Snow T; Diamond Light Source, Harwell Science Campus, Harwell, OX11 0DE, UK., Terrill NJ; Diamond Light Source, Harwell Science Campus, Harwell, OX11 0DE, UK., Knight MM; Centre for Bioengineering and School of Engineering and Materials Science, Queen Mary University of London, London, E1 4NS, UK., Gupta HS; Centre for Bioengineering and School of Engineering and Materials Science, Queen Mary University of London, London, E1 4NS, UK. |
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Jazyk: | angličtina |
Zdroj: | Advanced science (Weinheim, Baden-Wurttemberg, Germany) [Adv Sci (Weinh)] 2024 Nov 11, pp. e2407649. Date of Electronic Publication: 2024 Nov 11. |
DOI: | 10.1002/advs.202407649 |
Abstrakt: | By developing a 3D X-ray modeling and spatially correlative imaging method for fibrous collagenous tissues, this study provides a comprehensive mapping of nanoscale deformation in the collagen fibril network across the intact bone-cartilage unit (BCU), whose healthy functioning is critical for joint function and preventing degeneration. Extracting the 3D fibril structure from 2D small-angle X-ray scattering before and during physiological compression reveals of dominant deformation modes, including crystallinity transitions, lateral fibril compression, and reorientation, which vary in a coupled, nonlinear, and correlated manner across the cartilage-bone interface. A distinct intermolecular arrangement of collagen molecules, and enhanced molecular-level disorder, is found in the cartilage (sliding) surface region. Just below, fibrils accommodate tissue strain by reorientation, which transitions molecular-level kinking or loss of crystallinity in the deep zone. Crystalline fibrils laterally shrink far more (20×) than they contract, possibly by water loss from between tropocollagen molecules. With the calcified plate acting as an anchor for surrounding tissue, a qualitative switch occurs in fibrillar deformation between the articular cartilage and calcified regions. These findings significantly advance this understanding of the complex, nonlinear ultrastructural dynamics at this critical interface, and opens avenues for developing targeted diagnostic and therapeutic strategies for musculoskeletal disorders. (© 2024 The Author(s). Advanced Science published by Wiley‐VCH GmbH.) |
Databáze: | MEDLINE |
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