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Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs

Type I collagen physiological scaffold for tissue regeneration is considered one of the widely used biomaterials for tissue engineering and medical applications. It is hierarchically organized: five laterally staggered molecules are packed within fibrils, arranged into fascicles and bundles. The str...

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Autores principales: Terzi, Alberta, Gallo, Nunzia, Sibillano, Teresa, Altamura, Davide, Masi, Annalia, Lassandro, Rocco, Sannino, Alessandro, Salvatore, Luca, Bunk, Oliver, Giannini, Cinzia, De Caro, Liberato
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10342676/
https://www.ncbi.nlm.nih.gov/pubmed/37445069
http://dx.doi.org/10.3390/ma16134753
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author Terzi, Alberta
Gallo, Nunzia
Sibillano, Teresa
Altamura, Davide
Masi, Annalia
Lassandro, Rocco
Sannino, Alessandro
Salvatore, Luca
Bunk, Oliver
Giannini, Cinzia
De Caro, Liberato
author_facet Terzi, Alberta
Gallo, Nunzia
Sibillano, Teresa
Altamura, Davide
Masi, Annalia
Lassandro, Rocco
Sannino, Alessandro
Salvatore, Luca
Bunk, Oliver
Giannini, Cinzia
De Caro, Liberato
author_sort Terzi, Alberta
collection PubMed
description Type I collagen physiological scaffold for tissue regeneration is considered one of the widely used biomaterials for tissue engineering and medical applications. It is hierarchically organized: five laterally staggered molecules are packed within fibrils, arranged into fascicles and bundles. The structural organization is correlated to the direction and intensity of the forces which can be loaded onto the tissue. For a tissue-specific regeneration, the required macro- and microstructure of a suitable biomaterial has been largely investigated. Conversely, the function of multiscale structural integrity has been much less explored but is crucial for scaffold design and application. In this work, collagen was extracted from different animal sources with protocols that alter its structure. Collagen of tendon shreds excised from cattle, horse, sheep and pig was structurally investigated by wide- and small-angle X-ray scattering techniques, at both molecular and supramolecular scales, and thermo-mechanically with thermal and load-bearing tests. Tendons were selected because of their resistance to chemical degradation and mechanical stresses. The multiscale structural integrity of tendons’ collagen was studied in relation to the animal source, anatomic location and source for collagen extraction.
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spelling pubmed-103426762023-07-14 Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs Terzi, Alberta Gallo, Nunzia Sibillano, Teresa Altamura, Davide Masi, Annalia Lassandro, Rocco Sannino, Alessandro Salvatore, Luca Bunk, Oliver Giannini, Cinzia De Caro, Liberato Materials (Basel) Article Type I collagen physiological scaffold for tissue regeneration is considered one of the widely used biomaterials for tissue engineering and medical applications. It is hierarchically organized: five laterally staggered molecules are packed within fibrils, arranged into fascicles and bundles. The structural organization is correlated to the direction and intensity of the forces which can be loaded onto the tissue. For a tissue-specific regeneration, the required macro- and microstructure of a suitable biomaterial has been largely investigated. Conversely, the function of multiscale structural integrity has been much less explored but is crucial for scaffold design and application. In this work, collagen was extracted from different animal sources with protocols that alter its structure. Collagen of tendon shreds excised from cattle, horse, sheep and pig was structurally investigated by wide- and small-angle X-ray scattering techniques, at both molecular and supramolecular scales, and thermo-mechanically with thermal and load-bearing tests. Tendons were selected because of their resistance to chemical degradation and mechanical stresses. The multiscale structural integrity of tendons’ collagen was studied in relation to the animal source, anatomic location and source for collagen extraction. MDPI 2023-06-30 /pmc/articles/PMC10342676/ /pubmed/37445069 http://dx.doi.org/10.3390/ma16134753 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Terzi, Alberta
Gallo, Nunzia
Sibillano, Teresa
Altamura, Davide
Masi, Annalia
Lassandro, Rocco
Sannino, Alessandro
Salvatore, Luca
Bunk, Oliver
Giannini, Cinzia
De Caro, Liberato
Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs
title Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs
title_full Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs
title_fullStr Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs
title_full_unstemmed Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs
title_short Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs
title_sort travelling through the natural hierarchies of type i collagen with x-rays: from tendons of cattle, horses, sheep and pigs
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10342676/
https://www.ncbi.nlm.nih.gov/pubmed/37445069
http://dx.doi.org/10.3390/ma16134753
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