ABSTRACT
Flame retardancy is often required in various textile applications. Halogenated flame retardants (FR) are commonly used since they have good FR performance. Several of these components are listed under REACH. Halogen-free FR compounds have been developed as alternatives. So far, not many biobased FR have made it to the market and are being applied in the textile sector, leaving great opportunities since biobased products are experiencing a renaissance. In this study, renewable FR based on sorbitol and isosorbide were synthesised. The reaction was performed in the melt. The resulting biobased FR were characterised via FT-IR, thermogravimetric analysis (TGA) and X-ray fluorescence (XRF). Cotton fabrics functionalized with the developed biobased FR passed ISO 15025 FR test. After washing, the FR properties of the fabrics decreased (longer afterflame and afterglow time) but still complied with ISO 15025, indicating the biobased FR were semi-permanent. The amount of residue of modified sorbitol and isosorbide measured at 600 °C in air was 31% and 27%, respectively. Cotton treated with biobased modified FR showed no ignition during cone calorimetry experiments, indicating a flame retardancy. Furthermore, a charring of the FR containing samples was observed by means of cone calorimetry and TGA measurements.
ABSTRACT
Biomimetic mineralization of collagen is an advantageous method to obtain resorbable collagen/hydroxy-apatite composites for application in bone regeneration. In this report, established procedures for mineralization of bovine collagen were adapted to a new promising source of collagen from salmon skin challenged by the low denaturation temperature. Therefore, in the first instance, variation of temperature, collagen concentration, and ionic strength was performed to reveal optimized parameters for fibrillation and simultaneous mineralization of salmon collagen. Porous scaffolds from mineralized salmon collagen were prepared by controlled freeze-drying and chemical cross-linking. FT-IR analysis demonstrated the mineral phase formed during the preparation process to be hydroxyapatite. The scaffolds exhibited interconnecting porosity, were sufficiently stable under cyclic compression, and showed elastic mechanical properties. Human mesenchymal stem cells were able to adhere to the scaffolds, cell number increased during cultivation, and osteogenic differentiation was demonstrated in terms of alkaline phosphatase activity.
Subject(s)
Biomimetic Materials/chemistry , Bone Substitutes/chemistry , Collagen/chemistry , Tissue Engineering , Tissue Scaffolds/chemistry , Animals , Biomimetic Materials/chemical synthesis , Bone Substitutes/chemical synthesis , Cell Count , Cells, Cultured , Cross-Linking Reagents/chemical synthesis , Cross-Linking Reagents/chemistry , Humans , Mesenchymal Stem Cells/cytology , Particle Size , Porosity , Salmon , Surface PropertiesABSTRACT
Collagen is a popular biomaterial. To deal with its lack of thermal stability and its weak resistance to proteolytic degradation, collagen-based materials are stabilized via different cross-linking procedures. Regarding the potential toxicity of residual cross-linking agents, enzyme-mediated cross-linking would provide an alternative and nontoxic method for collagen stabilization. The results of this study show that type I collagen is a substrate for mTG. However, epsilon-(gamma-glutamyl)lysine cross-links are only incorporated at elevated temperatures when the protein is partially or completely denatured. A maximum number of 5.4 cross-links per collagen monomer were found for heat-denatured collagen. Labeling with the primary amine monodansylcadaverine revealed that at least half of the cross-links are located within the triple helical region of the collagen molecule. Because the triple helix is highly ordered in its native state, this finding might explain why the glutamine residues are inaccessible for mTG under nondenaturing conditions.
