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Tropocollagen springs allow collagen fibrils to stretch elastically

The mechanical properties of connective tissues are tailored to their specific function, and changes can lead to dysfunction and pathology. In most mammalian tissues the mechanical environment is governed by the micro- and nano-scale structure of collagen and its interaction with other tissue compon...

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Autores principales: Bell, James S., Hayes, Sally, Whitford, Charles, Sanchez-Weatherby, Juan, Shebanova, Olga, Terrill, Nick J., Sørensen, Thomas L.M., Elsheikh, Ahmed, Meek, Keith M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8982519/
https://www.ncbi.nlm.nih.gov/pubmed/35081430
http://dx.doi.org/10.1016/j.actbio.2022.01.041
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author Bell, James S.
Hayes, Sally
Whitford, Charles
Sanchez-Weatherby, Juan
Shebanova, Olga
Terrill, Nick J.
Sørensen, Thomas L.M.
Elsheikh, Ahmed
Meek, Keith M.
author_facet Bell, James S.
Hayes, Sally
Whitford, Charles
Sanchez-Weatherby, Juan
Shebanova, Olga
Terrill, Nick J.
Sørensen, Thomas L.M.
Elsheikh, Ahmed
Meek, Keith M.
author_sort Bell, James S.
collection PubMed
description The mechanical properties of connective tissues are tailored to their specific function, and changes can lead to dysfunction and pathology. In most mammalian tissues the mechanical environment is governed by the micro- and nano-scale structure of collagen and its interaction with other tissue components, however these hierarchical properties remain poorly understood. In this study we use the human cornea as a model system to characterise and quantify the dominant deformation mechanisms of connective tissue in response to cyclic loads of physiological magnitude. Synchronised biomechanical testing, x-ray scattering and 3D digital image correlation revealed the presence of two dominant mechanisms: collagen fibril elongation due to a largely elastic, spring-like straightening of tropocollagen supramolecular twist, and a more viscous straightening of fibril crimp that gradually increased over successive loading cycles. The distinct mechanical properties of the two mechanisms suggest they have separate roles in vivo. The elastic, spring-like mechanism is fast-acting and likely responds to stresses associated with the cardiac cycle, while the more viscous crimp mechanism will respond to slower processes, such as postural stresses. It is anticipated that these findings will have broad applicability to understanding the normal and pathological functioning of other connective tissues such as skin and blood vessels that exhibit both helical structures and crimp. STATEMENT OF SIGNIFICANCE: The tropocollagen spring mechanism allows collagen fibrils from some tissues to elongate significantly under small loads, and its recent discovery has the potential to change our fundamental understanding of how tissue deforms. This time-resolved study quantifies the contribution of the spring mechanism to the local strain in stretched tissue and compares it to the contribution associated with the straightening of fibril waviness, the widely accepted primary low-load strain mechanism. The spring mechanism contributed more to the local tissue strain than fibril straightening, and was found to be elastic while fibril straightening was more viscous. The results suggest that the viscoelastic behaviour of a biomaterial is controlled, at least in part, by the relative amount of fibril-scale crimp and tropocollagen supramolecular twist.
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spelling pubmed-89825192022-05-03 Tropocollagen springs allow collagen fibrils to stretch elastically Bell, James S. Hayes, Sally Whitford, Charles Sanchez-Weatherby, Juan Shebanova, Olga Terrill, Nick J. Sørensen, Thomas L.M. Elsheikh, Ahmed Meek, Keith M. Acta Biomater Full Length Article The mechanical properties of connective tissues are tailored to their specific function, and changes can lead to dysfunction and pathology. In most mammalian tissues the mechanical environment is governed by the micro- and nano-scale structure of collagen and its interaction with other tissue components, however these hierarchical properties remain poorly understood. In this study we use the human cornea as a model system to characterise and quantify the dominant deformation mechanisms of connective tissue in response to cyclic loads of physiological magnitude. Synchronised biomechanical testing, x-ray scattering and 3D digital image correlation revealed the presence of two dominant mechanisms: collagen fibril elongation due to a largely elastic, spring-like straightening of tropocollagen supramolecular twist, and a more viscous straightening of fibril crimp that gradually increased over successive loading cycles. The distinct mechanical properties of the two mechanisms suggest they have separate roles in vivo. The elastic, spring-like mechanism is fast-acting and likely responds to stresses associated with the cardiac cycle, while the more viscous crimp mechanism will respond to slower processes, such as postural stresses. It is anticipated that these findings will have broad applicability to understanding the normal and pathological functioning of other connective tissues such as skin and blood vessels that exhibit both helical structures and crimp. STATEMENT OF SIGNIFICANCE: The tropocollagen spring mechanism allows collagen fibrils from some tissues to elongate significantly under small loads, and its recent discovery has the potential to change our fundamental understanding of how tissue deforms. This time-resolved study quantifies the contribution of the spring mechanism to the local strain in stretched tissue and compares it to the contribution associated with the straightening of fibril waviness, the widely accepted primary low-load strain mechanism. The spring mechanism contributed more to the local tissue strain than fibril straightening, and was found to be elastic while fibril straightening was more viscous. The results suggest that the viscoelastic behaviour of a biomaterial is controlled, at least in part, by the relative amount of fibril-scale crimp and tropocollagen supramolecular twist. Elsevier 2022-04-01 /pmc/articles/PMC8982519/ /pubmed/35081430 http://dx.doi.org/10.1016/j.actbio.2022.01.041 Text en © 2022 The Authors. Published by Elsevier Ltd on behalf of Acta Materialia Inc. https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Full Length Article
Bell, James S.
Hayes, Sally
Whitford, Charles
Sanchez-Weatherby, Juan
Shebanova, Olga
Terrill, Nick J.
Sørensen, Thomas L.M.
Elsheikh, Ahmed
Meek, Keith M.
Tropocollagen springs allow collagen fibrils to stretch elastically
title Tropocollagen springs allow collagen fibrils to stretch elastically
title_full Tropocollagen springs allow collagen fibrils to stretch elastically
title_fullStr Tropocollagen springs allow collagen fibrils to stretch elastically
title_full_unstemmed Tropocollagen springs allow collagen fibrils to stretch elastically
title_short Tropocollagen springs allow collagen fibrils to stretch elastically
title_sort tropocollagen springs allow collagen fibrils to stretch elastically
topic Full Length Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8982519/
https://www.ncbi.nlm.nih.gov/pubmed/35081430
http://dx.doi.org/10.1016/j.actbio.2022.01.041
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