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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.
  • Terzi A; Institute of Crystallography, National Research Council, 70125 Bari, Italy.
  • Gallo N; Department of Engineering for Innovation, University of Salento, 73100 Lecce, Italy.
  • Sibillano T; Institute of Crystallography, National Research Council, 70125 Bari, Italy.
  • Altamura D; Institute of Crystallography, National Research Council, 70125 Bari, Italy.
  • Masi A; Department of Engineering for Innovation, University of Salento, 73100 Lecce, Italy.
  • Lassandro R; Institute of Crystallography, National Research Council, 70125 Bari, Italy.
  • Sannino A; Department of Engineering for Innovation, University of Salento, 73100 Lecce, Italy.
  • Salvatore L; Department of Engineering for Innovation, University of Salento, 73100 Lecce, Italy.
  • Bunk O; Typeone Biomaterials Srl, Via Europa 167, 73021 Calimera, Italy.
  • Giannini C; Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
  • De Caro L; Institute of Crystallography, National Research Council, 70125 Bari, Italy.
Materials (Basel) ; 16(13)2023 Jun 30.
Article en En | MEDLINE | ID: mdl-37445069
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.
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