The effect of collagen fibril orientation on the biphasic mechanics of articular cartilage
Damion, Robin A.
- Publisher: Elsevier
Articular cartilage | /dk/atira/pure/researchoutput/pubmedpublicationtype/D016428 | /dk/atira/pure/researchoutput/pubmedpublicationtype/D013485 | Biomedical Engineering | Collagen fibril | Biomechanics | Mechanics of Materials | Research Support, Non-U.S. Gov't | DT-MRI | Journal Article | Biomaterials | Fibril-reinforced biphasic model
mesheuropmc: macromolecular substances
<p>The highly inhomogeneous distribution of collagen fibrils may have important effects on the biphasic mechanics of articular cartilage. However, the effect of the inhomogeneity of collagen fibrils has mainly been investigated using simplified three-layered models, which may have underestimated the effect of collagen fibrils by neglecting their realistic orientation. The aim of this study was to investigate the effect of the realistic orientation of collagen fibrils on the biphasic mechanics of articular cartilage. Five biphasic material models, each of which included a different level of complexity of fibril reinforcement, were solved using two different finite element software packages (Abaqus and FEBio). Model 1 considered the realistic orientation of fibrils, which was derived from diffusion tensor magnetic resonance images. The simplified three-layered orientation was used for Model 2. Models 3–5 were three control models. The realistic collagen orientations obtained in this study were consistent with the literature. Results from the two finite element implementations were in agreement for each of the conditions modelled. The comparison between the control models confirmed some functions of collagen fibrils. The comparison between Models 1 and 2 showed that the widely-used three-layered inhomogeneous model can produce similar fluid load support to the model including the realistic fibril orientation; however, an accurate prediction of the other mechanical parameters requires the inclusion of the realistic orientation of collagen fibrils.</p>