Abstract
The aim of this work was to investigate the structural features of type I collagen isoforms and collagen-based films at atomic and molecular scales, in order to evaluate whether and to what extent different protocols of slurry synthesis may change the protein structure and the final properties of the developed scaffolds. Wide Angle X-ray Scattering data on raw materials demonstrated the preferential orientation of collagen molecules in equine tendon-derived collagens, while randomly oriented molecules were found in bovine skin collagens, together with a lower crystalline degree, analyzed by the assessment of FWHM (Full Width at Half Maximum), and a certain degree of salt contamination. WAXS and FT-IR (Fourier Transform Infrared) analyses on bovine collagen-based films, showed that mechanical homogenization of slurry in acidic solution was the treatment ensuring a high content of super-organization of collagen into triple helices and a high crystalline domain into the material. In vitro tests on rat Schwannoma cells showed that Schwann cell differentiation into myelinating cells was dependent on the specific collagen film being used, and was found to be stimulated in case of homogenization-treated samples. Finally DHT/EDC crosslinking treatment was shown to affect mechanical stiffness of films depending on collagen source and processing conditions.
Highlights
From a molecular point of view, type I collagen is a hetero trimer which consists of two α1 chains, encoded by COL1A1, and one α2 chain, encoded by COL1A23
Additional diffraction rings are clearly visible in CS and TYP-BH patterns (Fig. 2c,e), due to salt contamination of the raw material (i.e. NaCl), related to the extraction processes. 2D patterns were folded into 1D data profiles after the calibration procedure (Fig. 2)
From the analysis of the 1D profiles, two specific collagen reflections can be identified, as reported in the literature: the equatorial diffraction peak (q = 0.58 Å−1), that corresponds to an average apparent distance of 11 ± 2 Å between the triple helices in the quaternary structure; and a weak and wide meridional diffraction peak (q = 2.22 Å−1), that corresponds to a distance of 2.8 ± 2.0 Å between adjacent amino acid residues along the central axis of helical structure
Summary
From a molecular point of view, type I collagen is a hetero trimer which consists of two α1 chains, encoded by COL1A1, and one α2 chain, encoded by COL1A23. Gly is buried at the center of the triple helix The preservation of this amino acid in every third position of the triplet is required for close packing of the three helices that constitute the well-known triple helix structure[4]. The triple helix is a rod-like structure stabilized by hydrogen bonding, either direct (between the backbone NH group of glycine and the backbone CO group of a residue in the X position of the neighboring chain) or water mediated.
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