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Original Research ARTICLE Provisionally accepted The full-text will be published soon. Notify me

Front. Bioeng. Biotechnol. | doi: 10.3389/fbioe.2019.00203

Investigations of processing–induced structural changes in horse type-I collagen at sub and supramolecular levels

 Alberta Terzi1,  Nunzia Gallo2,  Simona Bettini3, Teresa Sibillano1, Davide Altamura1, Lorena Campa4,  Maria Lucia Natali4,  LUCA SALVATORE2, Marta Madaghiele2, Liberato De Caro1,  Ludovico Valli3,  Alessandro Sannino2 and  Cinzia Giannini5*
  • 1Institute of Crystallography (IC), Italy
  • 2Department of Innovation Engineering, University of Salento, Italy
  • 3Department of Biological and Environmental Sciences and Technologies, University of Salento, Italy
  • 4Typeone Srl, Italy
  • 5Italian National Research Council (CNR), Italy

The aim of this work was 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 occurring during fabrication protocols. Moreover, X rays analyses and Fourier Transform Infrared spectroscopy performed on the biomaterial shed light on the relation between processing conditions, triple helical content and organization in atomic and nanoscale domains. It was found that the mechanical homogenization of the slurry in acidic solution was the treatment ensuring a high content of super-organization of collagen into triple helices and a lower crystalline domain in the material. Finally, mechanical tensile tests were realized and proved that the acidic solution was the condition which most enhanced both mechanical stiffness and supramolecular fiber organization of the films.

Keywords: Collagen, SAXS (small-angle X-ray scattering), WAXS (Wide angle x-ray scattering), Mechani cal properties, FR-IR spectroscopy

Received: 30 May 2019; Accepted: 06 Aug 2019.

Copyright: © 2019 Terzi, Gallo, Bettini, Sibillano, Altamura, Campa, Natali, SALVATORE, Madaghiele, De Caro, Valli, Sannino and Giannini. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

* Correspondence: Dr. Cinzia Giannini, Italian National Research Council (CNR), Rome, Italy,