What is it about?

Collagen fibrils are important proteins in providing structural and mechanical stability in biological tissues. We have shown that a mutated form of these proteins has altered mechanics which were associated for the first time at the level of individual fibrils with the extend of hydration i.e. the uptake of water in the vicinity of the intrafibrilar matrix.

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Why is it important?

Our findings show the relationship between structure and mechanics at the individual fibril level of collagen and how hydration at the fibril level is altered due to changes in structure, i.e. the sequence of amino acids at the molecular level. We also show that the hydration is reduced in osteogenesis imperefecta collagen fibrils and that the reduced hydration was related to increased stiffness. Our experiments were also validated by computer simulations. These findings advance our knowledge on how collagen fibril structure and mechanics change due to a collagen-related pathology.

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This page is a summary of: Structure–mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model, Journal of The Royal Society Interface, October 2015, Royal Society Publishing,
DOI: 10.1098/rsif.2015.0701.
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