Biaxial mechanical/structural effects of equibiaxial strain during crosslinking of bovine pericardial xenograft materials

Langdon, S. E.; Chernecky, R.; Pereira, C. A.; Abdulla, D.; Lee, J M

doi:10.1016/s0142-9612(98)00142-2

Cited by 69 publications

(49 citation statements)

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“…During loading of collagen molecules, fibrils, and fibril bundles deform and finally fail by a process termed defibrillation. Up to a strain of 2% (toe region), stretching of the triple helix is the predominant mechanism of deformation [268][269][270][271] and corresponds to the gradual removal of a macroscopic crimp in the collagen fibrils [272][273][274][275][276][277][278][279][280][281]. This macroscopic crimp has been characterised as the shock absorber of tendons that permits non-damaging longitudinal elongation of fibrils within the tissue [261,282].…”

Section: Mechanical Properties Of Tendon Tissuementioning

confidence: 99%

The past, present and future in scaffold-based tendon treatments

Lomas

Ryan

Sorushanova

et al. 2015

Advanced Drug Delivery Reviews

183

188

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Section: Mechanical Properties Of Tendon Tissuementioning

confidence: 99%

The past, present and future in scaffold-based tendon treatments

Lomas

Ryan

Sorushanova

et al. 2015

Advanced Drug Delivery Reviews

183

188

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“…Morphological variations can be seen in the matrix surface after GA crosslinking. It is expected that different cross-linking procedures can modify the spatial organization of collagen fibrils and their surface topography [21] . The 0GA micrograph (Figure 5a) as a reference, exhibited a dense porous structure.…”

Section: Enviadomentioning

confidence: 99%

Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking

2010

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Abstract:In this work, the modifications promoted by alkaline hydrolysis and glutaraldehyde (GA) crosslinking on type I collagen found in porcine skin have been studied. Collagen matrices were obtained from the alkaline hydrolysis of porcine skin, with subsequent GA crosslinking in different concentrations and reaction times. The elastin content determination showed that independent of the treatment, elastin was present in the matrices. Results obtained from in vitro trypsin degradation indicated that with the increase of GA concentration and reaction time, the degradation rate decreased. From thermogravimetry and differential scanning calorimetry analysis it can be observed that the collagen in the matrices becomes more resistant to thermal degradation as a consequence of the increasing crosslink degree. Scanning electron microscopy analysis indicated that after the GA crosslinking, collagen fibers become more organized and well-defined. Therefore, the preparations of porcine skin matrices with different degradation rates, which can be used in soft tissue reconstruction, are viable.

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“…The bovine perichardial fixation with glutaraldehyde under biaxial static pressures (~225 and ~1875 mmHg) has been proposed. The bovine perichardium treated at high pressure showed an increase in stiffness and almost isotropic behaviour, while low pressure-treated bovine perichardium preserved the anisotropy exhibited by the native tissue (Langdon, et al, 1999). Porcine valves have also been subjected to crosslinking at high pressure (80 mm Hg), low and zero pressure.…”

Section: Tissue Crosslinking With Glutaraldehydementioning

confidence: 99%