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Home / Equine Research Bank / Front Bioeng Biotechnol / Investigations of Processing-Induced Structural Changes in H...
Frontiers in bioengineering and biotechnology2019; 7; 203; doi: 10.3389/fbioe.2019.00203

Investigations of Processing-Induced Structural Changes in Horse Type-I Collagen at Sub and Supramolecular Levels.

Abstract: The aim of this work is to evaluate the effects of different extraction and material processing protocols on the collagen structure and hierarchical organization of equine tendons. Wide and Small Angle X-ray Scattering investigations on raw powders and thin films revealed that not only the extraction and purification treatments, but also the processing conditions may affect the extent of the protein crystalline domain and induce a nanoscale "shield effect." This is due to the supramolecular fiber organization, which protects the atomic scale structure from the modifications that occur during fabrication protocols. Moreover, X-ray analyses and Fourier Transform Infrared spectroscopy performed on the biomaterial sheds light on the relationship between processing conditions, triple helical content and the organization in atomic and nanoscale domains. It was found that the mechanical homogenization of the slurry in acidic solution is a treatment that ensures a high content of super-organization of collagen into triple helices and a lower crystalline domain in the material. Finally, mechanical tensile tests were carried out, proving that the acidic solution is the condition which most enhances both mechanical stiffness and supramolecular fiber organization of the films.
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Publication Date: 2019-08-26 PubMed ID: 31552231PubMed Central: PMC6736615DOI: 10.3389/fbioe.2019.00203Google 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 article investigates the effects of different sample processing protocols on the structure and arrangement of horse tendon collagen — a common biomaterial used in medico-surgical applications. The scientists utilize X-ray Scattering techniques and Infrared spectroscopy to examine the changes induced at different structural levels, and relate these to mechanical properties of the resulting biomaterial.

Principal Objectives of the Research

  • Investigate the impact of extraction, purification, and processing conditions on the structural elements of horse tendon collagen, specifically on the protein’s crystalline domain and its arrangement of molecules.
  • Examine how processing conditions affect the formation of collagen’s triple helix structure and the arrangement at atomic and nanoscale levels.

Methodology and Analytical Techniques

  • Used Wide and Small Angle X-ray Scattering (WAXS & SAXS) to analyze powders and thin films of processed collagen. These techniques helped assess changes at different structural levels (from molecular to supramolecular).
  • Applied Fourier Transform Infrared (FTIR) spectroscopy on the collagen biomaterial. FTIR measures the infrared radiation absorbance stakes of molecular vibrations, providing insight into molecular structure and composition.
  • Performed mechanical tensile tests to gauge the mechanical stiffness and supramolecular fiber organization of the collagen films.

Key Findings of the Research

  • Identified that processing conditions, including the extraction and purification protocols, influence the size of the protein’s crystalline domain and can induce a protective nanoscale “shield effect”.
  • Established a connection between processing conditions and the formation of collagen’s triple helix structure — a crucial structural component for the functionality of the material in biotechnological applications.
  • Discovered that the mechanical homogenization of the collagen slurry in an acidic solution ensures a high super-organization of collagen into triple helices and a lower crystalline domain, thus optimizing collagen’s functionality and effectiveness as a biomaterial.
  • Confirmed through tensile tests that an acidic solution enhances the mechanical stiffness of the collagen and improves the supramolecular fiber organization of the films.

Cite This Article

APA
Terzi A, Gallo N, Bettini S, Sibillano T, Altamura D, Campa L, Natali ML, Salvatore L, Madaghiele M, De Caro L, Valli L, Sannino A, Giannini C. (2019). Investigations of Processing-Induced Structural Changes in Horse Type-I Collagen at Sub and Supramolecular Levels. Front Bioeng Biotechnol, 7, 203. https://doi.org/10.3389/fbioe.2019.00203

Publication

Frontiers in bioengineering and biotechnology
ISSN: 2296-4185
NlmUniqueID: 101632513
Country: Switzerland
Language: English
Volume: 7
Pages: 203
PII: 203

Researcher Affiliations

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

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Citations

This article has been cited 11 times.
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