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Citation

Thesis Title
The Effects Cross Linking on Collagen Type I Nanostructure and Nanostructural Response to Uniaxial Tension

Read article at Massey Research Online:

Collagen type I is the principal component in many natural tissues, commercial products and medical biomaterials. Such biomaterials are required to have specific properties which enable them to function as intended. The arrangement of collagen's fine structures and associated macromolecules impacts their bulk properties. Ms Kayed used synchrotron small angle X-ray scattering and microscopy techniques to determine the role of cross links in pericardium collagen nanostructure and mechanics. Glutaraldehyde cross links were found to alter collagen nanostructure and serve a mechanical function for direct stress transfer during uniaxial tension. In comparison, natural glycosaminoglycan cross links act as lubricants leading to increased fibril sliding. Neonatal and adult pericardium have the same propensity to be cross linked by glutaraldehyde. Her finding that the nature of cross links influences the response of collagen to tension by different mechanisms at the nanoscale may prove useful in the preparation of collagen materials across different fields.

Supervisors
Professor Richard Haverkamp
Associate Professor Gill Norris