Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs.
Abstract: 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.
Publication Date: 2023-06-30 PubMed ID: 37445069PubMed Central: PMC10342676DOI: 10.3390/ma16134753Google Scholar: Lookup
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Summary
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This study sets out to analyze the structural integrity of collagen at multiple scales, looking at the source of the collagen, its anatomical location, and how it was extracted. Using X-ray scattering techniques and various tests, the researchers investigated collagen molecules from the tendons of cattle, horses, sheep, and pigs.
Collagen and its Hierarchical Organization
- Collagen is a key biomaterial used in tissue engineering and various medical applications.
- It’s known for its unique hierarchical organization: five molecules are packed within fibrils, which are then arranged into fascicles and bundles.
- This structural organization is important because it is linked to the direction and intensity of forces that the tissue can withstand.
Investigating Collagen Structure
- The researchers focused on the multiscale structural integrity of collagen, which hasn’t been explored thoroughly yet but is crucial for designing and applying collagen scaffolds.
- To do this, they turned to different animal sources (cattle, horses, sheep, and pigs) and used different extraction protocols, each of which may alter the structure of the collagen.
- The tendons from these animals were chosen specifically for their resistance to both chemical degradation and mechanical stresses.
Techniques and Methods Used
- The researchers used wide- and small-angle X-ray scattering techniques to study these structural differences in the collagen samples at both the molecular and supramolecular scale.
- In addition to these X-ray techniques, thermal and load-bearing tests were performed to gain thermo-mechanical insights about the collagen’s structure.
Importance of Studying Collagen Structure Across Multiple Scales
- By assessing collagen’s multiscale structural integrity, researchers can generate valuable insights that could influence how collagen scaffolds are designed and used in clinical settings.
- Furthermore, revealing the potential differences in collagen structures based on their animal source or extraction method could help refine current biomaterial processes and protocols to optimize the use of collagen in various applications.
Cite This Article
APA
Terzi A, Gallo N, Sibillano T, Altamura D, Masi A, Lassandro R, Sannino A, Salvatore L, Bunk O, Giannini C, De Caro L.
(2023).
Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs.
Materials (Basel), 16(13).
https://doi.org/10.3390/ma16134753 Publication
Researcher Affiliations
- Institute of Crystallography, National Research Council, 70125 Bari, Italy.
- Department of Engineering for Innovation, University of Salento, 73100 Lecce, Italy.
- Institute of Crystallography, National Research Council, 70125 Bari, Italy.
- Institute of Crystallography, National Research Council, 70125 Bari, Italy.
- Department of Engineering for Innovation, University of Salento, 73100 Lecce, Italy.
- Institute of Crystallography, National Research Council, 70125 Bari, Italy.
- Department of Engineering for Innovation, University of Salento, 73100 Lecce, Italy.
- Department of Engineering for Innovation, University of Salento, 73100 Lecce, Italy.
- Typeone Biomaterials Srl, Via Europa 167, 73021 Calimera, Italy.
- Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
- Institute of Crystallography, National Research Council, 70125 Bari, Italy.
- Institute of Crystallography, National Research Council, 70125 Bari, Italy.
Grant Funding
- RIPARTI: POC PUGLIA FESR-FSE 2014/2020 , CUP B33C22000820002 / Regione Puglia
Conflict of Interest Statement
The authors declare no conflict of interest.
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