Biomechanical role of collagen cross-links in bone strength: finite element study

Abdelwahed Barkaoui (1) , Ridha Hambli (2) , Awad Bettamer (2)

1 PRISME - Laboratoire Pluridisciplinaire de Recherche en Ingénierie des Systèmes, Mécanique et Energétique
2 F2ME

Bone contains exclusively genetic Type I collagen. These collagens are identical sequences of amino acids that form the tropocollagen molecules linked by cross-links found at the end of each tropocollagen molecules. Collagen cross-linking, a major post-translational modification of collagen, plays important roles in the biological and biomechanical features of bone. The aim of this work is to use a 3D nano-scale finite element model of a sub structure in collagen fibril called mineralized collagen microfibril and to investigate the important roles of cross-links in the expression of bone strength and its capacity and ability to absorb energy. Studies in vitro and in vivo have reported that increases in cross-linking are associated with enhancement of some mechanical properties (strength and stiffness) and reductions of others (energy absorption).These experimental data are limited in their ability to define individual biomechanical effects of altered cross-linking. In the present work the study of the effect of cross-links is more realistic that's because the proposed finite element model success to combines the collagen, mineral and cross-links furthermore been able to varying the mechanical and geometry properties of each phase and to visualize their influence on corresponding equivalent properties of the collagen microfibril.

Mots clés: Bone; microfibril; cross-links; Finite elements

Domaines: Biomécanique [physics.med-ph]; Biomécanique [physics.med-ph]

Abdelwahed Barkaoui, Ridha Hambli, Awad Bettamer. Biomechanical role of collagen cross-links in bone strength: finite element study. ASBMR 2011, Sep 2011, San Diego, California, United States. ⟨hal-00654926⟩