Structure–mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model
The collagen molecule, which is the building block of collagen fibrils, is a triple helix of two α1(I) chains and one α2(I) chain. However, in the severe mouse model of osteogenesis imperfecta (OIM), deletion of the COL1A2 gene results in the substitution of the α2(I) chain by one α1(I) chain. As th...
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| Format: | Article |
| Language: | en_US |
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Royal Society
2016
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| Online Access: | http://hdl.handle.net/1721.1/101599 https://orcid.org/0000-0002-4173-9659 |
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| author | Andriotis, O. G. Chang, S. W. Vanleene, M. Howarth, P. H. Davies, D. E. Shefelbine, S. J. Thurner, P. J. Buehler, Markus J |
| author2 | Massachusetts Institute of Technology. Center for Materials Science and Engineering |
| author_facet | Massachusetts Institute of Technology. Center for Materials Science and Engineering Andriotis, O. G. Chang, S. W. Vanleene, M. Howarth, P. H. Davies, D. E. Shefelbine, S. J. Thurner, P. J. Buehler, Markus J |
| author_sort | Andriotis, O. G. |
| collection | MIT |
| description | The collagen molecule, which is the building block of collagen fibrils, is a triple helix of two α1(I) chains and one α2(I) chain. However, in the severe mouse model of osteogenesis imperfecta (OIM), deletion of the COL1A2 gene results in the substitution of the α2(I) chain by one α1(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. |
| first_indexed | 2024-09-23T13:46:43Z |
| format | Article |
| id | mit-1721.1/101599 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T13:46:43Z |
| publishDate | 2016 |
| publisher | Royal Society |
| record_format | dspace |
| spelling | mit-1721.1/1015992022-09-28T16:07:10Z Structure–mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model Andriotis, O. G. Chang, S. W. Vanleene, M. Howarth, P. H. Davies, D. E. Shefelbine, S. J. Thurner, P. J. Buehler, Markus J Massachusetts Institute of Technology. Center for Materials Science and Engineering Massachusetts Institute of Technology. Center for Computational Engineering Massachusetts Institute of Technology. Department of Civil and Environmental Engineering Massachusetts Institute of Technology. Laboratory for Atomistic and Molecular Mechanics Buehler, Markus J. The collagen molecule, which is the building block of collagen fibrils, is a triple helix of two α1(I) chains and one α2(I) chain. However, in the severe mouse model of osteogenesis imperfecta (OIM), deletion of the COL1A2 gene results in the substitution of the α2(I) chain by one α1(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. United States. Dept. of Defense. Presidential Early Career Award for Scientists and Engineers National Science Foundation (U.S.) (CAREER Award) 2016-03-04T16:07:16Z 2016-03-04T16:07:16Z 2015-10 2015-08 Article http://purl.org/eprint/type/JournalArticle 1742-5689 1742-5662 http://hdl.handle.net/1721.1/101599 Andriotis, O. G., S. W. Chang, M. Vanleene, P. H. Howarth, D. E. Davies, S. J. Shefelbine, M. J. Buehler, and P. J. Thurner. “Structure–mechanics Relationships of Collagen Fibrils in the Osteogenesis Imperfecta Mouse Model.” Journal of The Royal Society Interface 12, no. 111 (October 6, 2015): 20150701. https://orcid.org/0000-0002-4173-9659 en_US http://dx.doi.org/10.1098/rsif.2015.0701 Journal of The Royal Society Interface Creative Commons Attribution http://creativecommons.org/licenses/by/4.0/ application/pdf Royal Society The Royal Society |
| spellingShingle | Andriotis, O. G. Chang, S. W. Vanleene, M. Howarth, P. H. Davies, D. E. Shefelbine, S. J. Thurner, P. J. Buehler, Markus J Structure–mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model |
| title | Structure–mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model |
| title_full | Structure–mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model |
| title_fullStr | Structure–mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model |
| title_full_unstemmed | Structure–mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model |
| title_short | Structure–mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model |
| title_sort | structure mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model |
| url | http://hdl.handle.net/1721.1/101599 https://orcid.org/0000-0002-4173-9659 |
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