Khaled Hijazi | University of Western Ontario (original) (raw)

Khaled Hijazi

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Papers by Khaled Hijazi

Research paper thumbnail of Ultrastructural response of tendon to excessive level or duration of tensile load supports that collagen fibrils are mechanically continuous

Journal of the Mechanical Behavior of Biomedical Materials, 2019

The basic collagen fibril structure of tendons continues to be debated in the literature. Some st... more The basic collagen fibril structure of tendons continues to be debated in the literature. Some studies have proposed that collagen fibrils are longitudinally discontinuous, with the load-bearing ability of tendon dependent on interfibrillar shear strength. Other evidence indicates that collagen fibrils are probably structurally continuous, running uninterrupted from osteotendinous to myotendinous junction. In this study we explored the question of collagen fibril continuity in tendon by examining fibril response to tendon loading. Tendons were subjected to high stress and/or long duration tensile loading routines, after which we examined the ultrastructure of the tendons using differential scanning calorimetry and scanning electron microscopy, comparing the results from the loaded tendons to control samples taken from the same tendons prior to loading. Our results show that under ramp loading, collagen fibril damage begins near the end of the linear region in the stress-strain response (i.e., near the yield point). When tendons are allowed to gradually elongate under static load, tendon rupture is caused by failure of collagen fibrils, not uncontrolled slippage between fibrils. Our findings indicate that the collagen fibrils of tendon are at least sufficiently long to be mechanically continuous, meaning that tensile failure of tendon does not occur as the result of uncontrolled slippage between fibrils, but by failure of the fibrils themselves.

Research paper thumbnail of Effect of creep loading on the nanostructure of tendons

xi, 123 leaves : illustrations (some coloured) ; 29 cmIncludes abstract.Includes bibliographical ... more xi, 123 leaves : illustrations (some coloured) ; 29 cmIncludes abstract.Includes bibliographical references (leaves 113-123).This thesis focused on exploring ultrastructural damage to tendons during low strain-rate loading at overload and suboverload levels. In the first experiment, tendons were either statically loaded at overload stress until rupture, ramp loaded to yield and then unloaded, or ramp loaded until rupture. In the second experiment, tendons were statically loaded at suboverloaded stress for different periods of time, after which they were unloaded. Structural assessments of loaded tendons and matched-pair controls were conducted using scanning electron microscopy and differential scanning calorimetry. Rupturing tendons at low strain-rate created significant ultrastructural damage to the packing of collagen molecules within fibrils. Only when rupture occurred during static loading, though, were significant quantities of denatured collagen created. Sustained loading at suboverload levels was found to disrupt collagen fibrils when applied for durations >2 hours

Research paper thumbnail of Ultrastructural response of tendon to excessive level or duration of tensile load supports that collagen fibrils are mechanically continuous

Journal of the Mechanical Behavior of Biomedical Materials, 2019

The basic collagen fibril structure of tendons continues to be debated in the literature. Some st... more The basic collagen fibril structure of tendons continues to be debated in the literature. Some studies have proposed that collagen fibrils are longitudinally discontinuous, with the load-bearing ability of tendon dependent on interfibrillar shear strength. Other evidence indicates that collagen fibrils are probably structurally continuous, running uninterrupted from osteotendinous to myotendinous junction. In this study we explored the question of collagen fibril continuity in tendon by examining fibril response to tendon loading. Tendons were subjected to high stress and/or long duration tensile loading routines, after which we examined the ultrastructure of the tendons using differential scanning calorimetry and scanning electron microscopy, comparing the results from the loaded tendons to control samples taken from the same tendons prior to loading. Our results show that under ramp loading, collagen fibril damage begins near the end of the linear region in the stress-strain response (i.e., near the yield point). When tendons are allowed to gradually elongate under static load, tendon rupture is caused by failure of collagen fibrils, not uncontrolled slippage between fibrils. Our findings indicate that the collagen fibrils of tendon are at least sufficiently long to be mechanically continuous, meaning that tensile failure of tendon does not occur as the result of uncontrolled slippage between fibrils, but by failure of the fibrils themselves.

Research paper thumbnail of Effect of creep loading on the nanostructure of tendons

xi, 123 leaves : illustrations (some coloured) ; 29 cmIncludes abstract.Includes bibliographical ... more xi, 123 leaves : illustrations (some coloured) ; 29 cmIncludes abstract.Includes bibliographical references (leaves 113-123).This thesis focused on exploring ultrastructural damage to tendons during low strain-rate loading at overload and suboverload levels. In the first experiment, tendons were either statically loaded at overload stress until rupture, ramp loaded to yield and then unloaded, or ramp loaded until rupture. In the second experiment, tendons were statically loaded at suboverloaded stress for different periods of time, after which they were unloaded. Structural assessments of loaded tendons and matched-pair controls were conducted using scanning electron microscopy and differential scanning calorimetry. Rupturing tendons at low strain-rate created significant ultrastructural damage to the packing of collagen molecules within fibrils. Only when rupture occurred during static loading, though, were significant quantities of denatured collagen created. Sustained loading at suboverload levels was found to disrupt collagen fibrils when applied for durations >2 hours

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