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.
Highlights
Tissue engineering is based on the implantation of biocompatible and biodegradable scaffolds that provides structural support to cell growth and tissue development
Wide Angle X-rays Scattering technique reveals a preferential orientation of molecules in raw TYP1 collagens compared to collagen control (CC), but the extent of the crystalline domains is not affected by the extraction and purification treatment
Film fabrication protocols affect the structural properties of the material in different ways, depending on the extent of supramolecular hierarchy, which is in turn related to the extraction protocols
Summary
Tissue engineering is based on the implantation of biocompatible and biodegradable scaffolds that provides structural support to cell growth and tissue development. The goal is to mimic the microenvironment architecture, mainly represented by the extracellular matrix (ECM), a complex network composed by water and strongly interconnected fibrous/non-fibrous proteins and polysaccharides, that supports tissue growth and mechanical stability and allows optimal homeostasis (Kim et al, 2016). Variations of the ECM biological and mechanical structure have been demonstrated among different tissues, such as skin and tendon, and among different areas of the same organ, and different pathologic states (Frantz et al, 2010). The covalent bonds between amine and carboxyl groups within molecules are mainly located in these regions, stabilizing the molecular arrangement by crosslinking
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