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Macromolecular bioscience2020; 20(5); e2000017; doi: 10.1002/mabi.202000017

Sub- and Supramolecular X-Ray Characterization of Engineered Tissues from Equine Tendon, Bovine Dermis, and Fish Skin Type-I Collagen.

Abstract: Collagen represents one of the most widely used biomaterial for scaffolds fabrication in tissue engineering as it represents the mechanical support of natural tissues. It also provides physical scaffolding for cells and it influences their attachment, growth, and tissue regeneration. Among all fibrillary collagens, type I is considered one of the gold standard for scaffolds fabrication, thanks to its high biocompatibility, biodegradability, and hemostatic properties. It can be extracted by chemical and enzymatic protocols from several collagen-rich tissues, such as tendon and skin, of different animal species. Both the extraction processes and the manufacturing protocols for scaffolds fabrication provide structural and mechanical changes that can be tuned in order to deeply impact the properties of the final biomaterial. The aim of this review is to discuss the role of X-rays to study structural changes of type I collagen from fresh collagen-rich tissues (bovine, equine, fish) to the final scaffolds, with the aim to screen across available collagen sources and scaffolds fabrication protocols to be used in tissue regeneration.
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Publication Date: 2020-03-12 PubMed ID: 32163225DOI: 10.1002/mabi.202000017Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research focuses on the use of X-ray characterization to study the structural changes in type I collagen, a popular biomaterial for scaffold fabrication in tissue engineering, as it transforms from its original state in various collagen-rich tissues (bovine, equine, fish) to the final scaffolds used in tissue regeneration.

Use of Type I Collagen in Tissue Engineering

  • The study revolves around the importance of type I collagen in tissue engineering, a field of medical science that involves the development of biological substitutes or scaffolds to repair or replace damaged tissue.
  • Type I collagen, abundantly present in multiple tissues of different animal species such as tendons and skin, is often used to engineer scaffolds due to its high biocompatibility, biodegradability, and hemostatic properties, all of which contribute to enhancing the efficiency of tissue regeneration.

Extraction and Manufacturing Process

  • Typically extracted using chemical and enzymatic protocols, the structure and mechanical strength of type I collagen can be altered in the extraction process and the subsequent manufacturing protocols for scaffold production.
  • These structural and mechanical changes can be manipulated in various ways to significantly affect the final properties of the biomaterial. This tunability of collagen’s properties is crucial for tailoring the material to specific applications in tissue regeneration.

X-ray Characterization of Engineered Tissues

  • The primary objective of the research is to illuminate the role of X-rays in the detailed study of structural changes of type I collagen that occurs from fresh collagen-rich tissues to the final scaffolds.
  • Through X-ray characterization, one can screen across available sources of collagen and varying scaffold fabrication processes, providing a greater understanding of how each stage impacts the functionality of the resulting biomaterial in tissue regeneration.
  • The findings might contribute to the identification of the best collagen sources and scaffold production techniques, ultimately improving the effectiveness of tissue engineering practices.

Cite This Article

APA
Terzi A, Gallo N, Bettini S, Sibillano T, Altamura D, Madaghiele M, De Caro L, Valli L, Salvatore L, Sannino A, Giannini C. (2020). Sub- and Supramolecular X-Ray Characterization of Engineered Tissues from Equine Tendon, Bovine Dermis, and Fish Skin Type-I Collagen. Macromol Biosci, 20(5), e2000017. https://doi.org/10.1002/mabi.202000017

Publication

Macromolecular bioscience
ISSN: 1616-5195
NlmUniqueID: 101135941
Country: Germany
Language: English
Volume: 20
Issue: 5
Pages: e2000017

Researcher Affiliations

Terzi, Alberta
  • Institute of Crystallography (IC), National Research Council, Bari, 70126, Italy.
Gallo, Nunzia
  • Department of Engineering for Innovation, University of Salento, Lecce, 73100, Italy.
Bettini, Simona
  • Department of Engineering for Innovation, University of Salento, Lecce, 73100, Italy.
Sibillano, Teresa
  • Institute of Crystallography (IC), National Research Council, Bari, 70126, Italy.
Altamura, Davide
  • Institute of Crystallography (IC), National Research Council, Bari, 70126, Italy.
Madaghiele, Marta
  • Department of Engineering for Innovation, University of Salento, Lecce, 73100, Italy.
De Caro, Liberato
  • Institute of Crystallography (IC), National Research Council, Bari, 70126, Italy.
Valli, Ludovico
  • Department of Biological and Environmental Sciences and Technologies, University of Salento, Lecce, 73100, Italy.
Salvatore, Luca
  • Department of Engineering for Innovation, University of Salento, Lecce, 73100, Italy.
Sannino, Alessandro
  • Department of Engineering for Innovation, University of Salento, Lecce, 73100, Italy.
Giannini, Cinzia
  • Institute of Crystallography (IC), National Research Council, Bari, 70126, Italy.

MeSH Terms

  • Animals
  • Cattle
  • Collagen Type I / metabolism
  • Dermis / diagnostic imaging
  • Fishes
  • Horses
  • Skin / diagnostic imaging
  • Tendons / diagnostic imaging
  • Tissue Engineering
  • X-Rays

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Citations

This article has been cited 28 times.
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