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1.
Connect Tissue Res ; 59(4): 345-355, 2018 07.
Artigo em Inglês | MEDLINE | ID: mdl-29083939

RESUMO

Purpose and Aims: Sea urchin teeth consist of calcite and form in two stages with different magnesium contents. The first stage structures of independently formed plates and needle-prisms define the shape of the tooth, and the columns of the second stage mineral cements the first stage structures together and control the fracture behavior of the mature tooth. This study investigates the nucleation and growth of the second stage mineral. MATERIALS AND METHODS: Scanning electron microscopy (SEM) and synchrotron microComputed Tomography characterized the structures of the second phase material found in developing of Lytechinus variegatus teeth. RESULTS: Although the column development is a continuous process, defining four phases of column formation captures the changes that occur in teeth of L. variegatus. The earliest phase consists of small 1-2 µm diameter hemispheres, and the second of 5-10 µm diameter, mound-like structures with a nodular surface, develops from the hemispheres. The mounds eventually bridge the syncytium between adjacent plates and form hyperboloid structures (phase three) that appear like mesas when plates separate during the fracture. The mesa diameter increases with time until the column diameter is significantly larger than its height, defining the fourth phase of column development. Energy dispersive x-ray spectroscopy confirms that the columns contain more magnesium than the underlying plates; the ratios of magnesium to calcium are consistent with compositions derived from x-ray diffraction. CONCLUSION: Columns grow from both bounding plates. The presence of first phase columns interspersed among third stage mesas indicates very localized control of mineralization.


Assuntos
Lytechinus/química , Minerais/química , Animais , Elétrons , Lytechinus/ultraestrutura , Espectrometria por Raios X , Microtomografia por Raio-X
2.
J Mech Behav Biomed Mater ; 152: 106464, 2024 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-38367533

RESUMO

A significant deformation mechanism of collagen at low loads is molecular uncoiling and rearrangement. Although the effect of hydration and cross-linking has been investigated at larger loads when collagen undergoes molecular sliding, their effects on collagen molecular reorganization remain unclear. Here we develop two thermodynamic models that use the notion of open-system elasticity to elucidate the effect of swelling due to water uptake during deformation of collagen networks under low and high cross-linking conditions. With low crosslinking, entropic contributions dominate resulting in rejection of solvent from the polymer network leading to reduced collagen stiffness with increased loads. Contrarily, high cross-linking inhibits initial coiling and structural kinking and the mechanical behavior is dominated by elastic energy. In this configuration, the solvent content depends on the sign of the applied load resulting in a non-linear open-system stress-strain relationship. The models provide insight on the parameters that impact the stress-strain relationships of hydrated collagen and can inform the way collagenous matrices are treated both in medical and laboratory settings.


Assuntos
Colágeno , Água , Solventes , Elasticidade , Transporte Biológico
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