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Biology2022; 11(8); 1096; doi: 10.3390/biology11081096

Structure and Strength of Bovine and Equine Amniotic Membrane.

Abstract: Thin, strong scaffold materials are needed for surgical applications. New materials are required, particularly those readily available, such as from non-human sources. Bovine amniotic membrane (antepartum) and equine amniotic membrane (postpartum) were characterized with tear and tensile tests. The structural arrangement of the collagen fibrils was determined by small-angle X-ray scattering, scanning electron microscopy, and ultrasonic imaging. Bovine amnion had a thickness-normalized tear strength of 12.6 (3.8) N/mm, while equine amnion was 14.8 (5.3) N/mm. SAXS analysis of the collagen fibril arrangement yielded an orientation index of 0.587 (0.06) and 0.681 (0.05) for bovine and equine, respectively. This may indicate a relationship between more highly aligned collagen fibrils and greater strength, as seen in other materials. Amnion from bovine or equine sources are strong, thin, elastic materials, although weaker than other collagen tissue materials commonly used, that may find application in surgery as an alternative to material from human donors.
Publication Date: 2022-07-23 PubMed ID: 35892952PubMed Central: PMC9329871DOI: 10.3390/biology11081096Google Scholar: Lookup
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  • Journal Article

Summary

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The research investigated the structure and strength of bovine (cow) and equine (horse) amniotic membranes with potential surgical applications. These thin, strong materials from non-human sources could prove useful in creating new supplies for various medical procedures.

Analysis and Testing Methods

  • The study tested the tear and tensile strength of both bovine (antepartum) and equine (postpartum) amniotic membranes. Tear and tensile tests measure the force required to pull a material apart, indicating its resistance to tearing and its overall strength respectively.
  • The researchers used small-angle X-ray scattering (SAXS), scanning electron microscopy, and ultrasonic imaging to determine the structural arrangement of collagen fibrils. Collagen fibrils, a necessary component of connective tissues in essentially all multi-cellular organisms, are the primary constituent of these membranes and their arrangement is fundamentally related to their functional properties.

Findings from the Study

  • The bovine amnion showed a thickness-normalized tear strength of 12.6 (3.8) N/mm, while the equine amnion measured at 14.8 (5.3) N/mm. These values suggest that these membranes are quite resilient and capable of withstanding substantial forces.
  • SAXS analysis showed that the collagen fibril arrangement in both bovine and equine amniotic membranes were highly aligned. Bovine amniotic membrane had an orientation index of 0.587 (0.06), while the equine amniotic membrane measured at 0.681 (0.05). This high degree of alignment would generally imply that the material would exhibit strong tensile strength.
  • The findings suggest a possible relationship between the greater alignment of collagen fibrils and increased strength in these membranes, a trend identified in other material studies.

Implications for Surgical Applications

  • Amnion from bovine or equine sources are strong, thin, elastic materials, even though they are weaker than other commonly used collagen tissue materials.
  • These properties make them potential candidates for use in surgical procedures as an alternative to materials from human donors. Grafting these tissues into humans may provide a significant advantage in their availability as they can be regularly collected from animals without ethical or supply concerns associated with human donors.

Cite This Article

APA
Wells HC, Sizeland KH, Kirby N, Haverkamp RG. (2022). Structure and Strength of Bovine and Equine Amniotic Membrane. Biology (Basel), 11(8), 1096. https://doi.org/10.3390/biology11081096

Publication

ISSN: 2079-7737
NlmUniqueID: 101587988
Country: Switzerland
Language: English
Volume: 11
Issue: 8
PII: 1096

Researcher Affiliations

Wells, Hannah C
  • School of Food and Advanced Technology, Massey University, Palmerston North 4442, New Zealand.
Sizeland, Katie H
  • ANSTO, Lucas Heights, NSW 2234, Australia.
  • ANSTO, Clayton, VIC 3168, Australia.
Kirby, Nigel
  • ANSTO, Clayton, VIC 3168, Australia.
Haverkamp, Richard G
  • School of Food and Advanced Technology, Massey University, Palmerston North 4442, New Zealand.

Grant Funding

  • M10652 / Australian Nuclear Science and Technology Organisation

Conflict of Interest Statement

The authors declare no conflict of interest.

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