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Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum
This study aims to provide understanding of the macroscopic viscoelastic behavior of collagen matrices through studying the relaxation time distribution spectrum obtained from stress relaxation tests. Hydrated collagen gel and dehydrated collagen thin film was exploited as two different hydration le...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3749280/ https://www.ncbi.nlm.nih.gov/pubmed/23628869 http://dx.doi.org/10.4161/biom.24651 |
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author | Xu, Bin Li, Haiyue Zhang, Yanhang |
author_facet | Xu, Bin Li, Haiyue Zhang, Yanhang |
author_sort | Xu, Bin |
collection | PubMed |
description | This study aims to provide understanding of the macroscopic viscoelastic behavior of collagen matrices through studying the relaxation time distribution spectrum obtained from stress relaxation tests. Hydrated collagen gel and dehydrated collagen thin film was exploited as two different hydration levels of collagen matrices. Genipin solution was used to induce crosslinking in collagen matrices. Biaxial stress relaxation tests were performed to characterize the viscoelastic behavior of collagen matrices. The rate of stress relaxation of both hydrated and dehydrated collagen matrices shows a linear initial stress level dependency. Increased crosslinking reduces viscosity in collagen gel, but the effect is negligible for thin film. Relaxation time distribution spectrum was obtained from the stress relaxation data by inverse Laplace transform. For most of the collagen matrices, three peaks at the short (0.3s ~1 s), medium (3s ~90 s), and long relaxation time (> 200 s) were observed in the continuous spectrum, which likely corresponds to relaxation mechanisms involve fiber, inter-fibril, and fibril sliding. Splitting of the middle peak was observed at higher initial stress levels suggesting increased structural heterogeneity at the fibril level with mechanical loading. The intensity of the long-term peaks increases with higher initial stress levels indicating the engagement of collagen fibrils at higher levels of tissue strain. |
format | Online Article Text |
id | pubmed-3749280 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-37492802013-08-29 Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum Xu, Bin Li, Haiyue Zhang, Yanhang Biomatter Special Focus Report This study aims to provide understanding of the macroscopic viscoelastic behavior of collagen matrices through studying the relaxation time distribution spectrum obtained from stress relaxation tests. Hydrated collagen gel and dehydrated collagen thin film was exploited as two different hydration levels of collagen matrices. Genipin solution was used to induce crosslinking in collagen matrices. Biaxial stress relaxation tests were performed to characterize the viscoelastic behavior of collagen matrices. The rate of stress relaxation of both hydrated and dehydrated collagen matrices shows a linear initial stress level dependency. Increased crosslinking reduces viscosity in collagen gel, but the effect is negligible for thin film. Relaxation time distribution spectrum was obtained from the stress relaxation data by inverse Laplace transform. For most of the collagen matrices, three peaks at the short (0.3s ~1 s), medium (3s ~90 s), and long relaxation time (> 200 s) were observed in the continuous spectrum, which likely corresponds to relaxation mechanisms involve fiber, inter-fibril, and fibril sliding. Splitting of the middle peak was observed at higher initial stress levels suggesting increased structural heterogeneity at the fibril level with mechanical loading. The intensity of the long-term peaks increases with higher initial stress levels indicating the engagement of collagen fibrils at higher levels of tissue strain. Landes Bioscience 2013-07-01 2013-04-01 /pmc/articles/PMC3749280/ /pubmed/23628869 http://dx.doi.org/10.4161/biom.24651 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Special Focus Report Xu, Bin Li, Haiyue Zhang, Yanhang Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum |
title | Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum |
title_full | Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum |
title_fullStr | Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum |
title_full_unstemmed | Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum |
title_short | Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum |
title_sort | understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum |
topic | Special Focus Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3749280/ https://www.ncbi.nlm.nih.gov/pubmed/23628869 http://dx.doi.org/10.4161/biom.24651 |
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