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Structure-mechanics relationships of collagen fibrils in the osteogenesis imperfect mouse model

Structure-mechanics relationships of collagen fibrils in the osteogenesis imperfect mouse model
Structure-mechanics relationships of collagen fibrils in the osteogenesis imperfect mouse model
The collagen molecule, which is the building block of collagen fibrils, is a triple helix of two ?1(I) chains and one ?2(I) chain. However, in the severe mouse model of osteogenesis imperfecta (OIM), deletion of the COL1A2 gene results in the substitution of the ?2(I) chain by one ?1(I) chain. As this substitution severely impairs the structure and mechanics of collagen-rich tissues at the tissue and organ level, the main aim of this study was to investigate how the structure and mechanics are altered in OIM collagen fibrils. Comparing results from atomic force microscopy imaging and cantilever-based nanoindentation on collagen fibrils from OIM and wild-type (WT) animals, we found a 33% lower indentation modulus in OIM when air-dried (bound water present) and an almost fivefold higher indentation modulus in OIM collagen fibrils when fully hydrated (bound and unbound water present) in phosphate-buffered saline solution (PBS) compared with WT collagen fibrils. These mechanical changes were accompanied by an impaired swelling upon hydration within PBS. Our experimental and atomistic simulation results show how the structure and mechanics are altered at the individual collagen fibril level as a result of collagen gene mutation in OIM. We envisage that the combination of experimental and modelling approaches could allow mechanical phenotyping at the collagen fibril level of virtually any alteration of collagen structure or chemistry.
collagen, structure, mechanics, osteogenesis imperfecta, atomic foce microspopy, atomistic simulations
Andriotis, O.G.
c94b057f-5bee-4558-81ce-8bb070cbf8dc
Chang, S.W.
ebad23e0-af20-466f-9ea6-8863b7ef57a4
Vanleene, M.
f5c77a3b-ac62-4378-a1cc-41c30259bf21
Howarth, P.H.
ff19c8c4-86b0-4a88-8f76-b3d87f142a21
Davies, D.E.
7de8fdc7-3640-4e3a-aa91-d0e03f990c38
Shefelbine, S.J.
1153780e-939e-4658-9ebe-f03db4155188
Buehler, M.J.
7845eef0-0846-4734-869e-17e0868d6402
Thurner, P.J.
131fcb70-883d-43f9-96d5-ddf6c566df1f
Andriotis, O.G.
c94b057f-5bee-4558-81ce-8bb070cbf8dc
Chang, S.W.
ebad23e0-af20-466f-9ea6-8863b7ef57a4
Vanleene, M.
f5c77a3b-ac62-4378-a1cc-41c30259bf21
Howarth, P.H.
ff19c8c4-86b0-4a88-8f76-b3d87f142a21
Davies, D.E.
7de8fdc7-3640-4e3a-aa91-d0e03f990c38
Shefelbine, S.J.
1153780e-939e-4658-9ebe-f03db4155188
Buehler, M.J.
7845eef0-0846-4734-869e-17e0868d6402
Thurner, P.J.
131fcb70-883d-43f9-96d5-ddf6c566df1f

Andriotis, O.G., Chang, S.W., Vanleene, M., Howarth, P.H., Davies, D.E., Shefelbine, S.J., Buehler, M.J. and Thurner, P.J. (2015) Structure-mechanics relationships of collagen fibrils in the osteogenesis imperfect mouse model. Journal of the Royal Society Interface, 12 (111). (doi:10.1098/rsif.2015.0701). (PMID:26468064)

Record type: Article

Abstract

The collagen molecule, which is the building block of collagen fibrils, is a triple helix of two ?1(I) chains and one ?2(I) chain. However, in the severe mouse model of osteogenesis imperfecta (OIM), deletion of the COL1A2 gene results in the substitution of the ?2(I) chain by one ?1(I) chain. As this substitution severely impairs the structure and mechanics of collagen-rich tissues at the tissue and organ level, the main aim of this study was to investigate how the structure and mechanics are altered in OIM collagen fibrils. Comparing results from atomic force microscopy imaging and cantilever-based nanoindentation on collagen fibrils from OIM and wild-type (WT) animals, we found a 33% lower indentation modulus in OIM when air-dried (bound water present) and an almost fivefold higher indentation modulus in OIM collagen fibrils when fully hydrated (bound and unbound water present) in phosphate-buffered saline solution (PBS) compared with WT collagen fibrils. These mechanical changes were accompanied by an impaired swelling upon hydration within PBS. Our experimental and atomistic simulation results show how the structure and mechanics are altered at the individual collagen fibril level as a result of collagen gene mutation in OIM. We envisage that the combination of experimental and modelling approaches could allow mechanical phenotyping at the collagen fibril level of virtually any alteration of collagen structure or chemistry.

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Accepted/In Press date: 24 September 2015
e-pub ahead of print date: 6 October 2015
Keywords: collagen, structure, mechanics, osteogenesis imperfecta, atomic foce microspopy, atomistic simulations
Organisations: Clinical & Experimental Sciences

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Local EPrints ID: 390337
URI: https://eprints.soton.ac.uk/id/eprint/390337
PURE UUID: ab6e5e7b-9a66-46d2-aa05-b24a7a04a1f0

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Date deposited: 24 Mar 2016 11:40
Last modified: 06 Nov 2017 17:31

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Contributors

Author: O.G. Andriotis
Author: S.W. Chang
Author: M. Vanleene
Author: P.H. Howarth
Author: D.E. Davies
Author: S.J. Shefelbine
Author: M.J. Buehler
Author: P.J. Thurner

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