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Gelatin powder substitute5/26/2023 The frozen samples were freeze-dried (Ilshin, Dongducheonsi, Republic of Korea) for 24 to 48 h until fully dried, followed by crosslinking with genipin through immersion in a 0.1% ( w/ v) genipin solution for 6 h. The solutions were then pipetted into a specific mould and frozen at −80 ☌ for 6 h. The solutions were allowed to stir until a uniform suspension of CNC was achieved. Upon dissolving the elastin powder, different concentrations of CNC were added into separate gelatin–elastin mixtures. Elastin was added to the mixture at a concentration of 0.2% ( w/ v). The stock solution was then mixed until all the powders had been dissolved. Ī stock solution containing 5% ( w/ v) gelatin was first prepared by dissolving Nitta-Gelatin powder in distilled water with constant stirring at a temperature of 40 ☌. To overcome these limitations, gelatin requires either crosslinking or reinforcement with other polymers to form a hybrid or composite. Despite its diverse benefits, gelatin is hindered by its lack of enzymatic and thermal resistance, as well as its mechanical weakness. Gelatin has been used to coat cell culture plates and construct scaffolds due to its cell binding capacity, biocompatibility, and biodegradability. Although gelatin is mainly derived from animals, its denatured property confers it with very low antigenicity, and it produces harmless metabolic products post degradation. Unlike collagen, it is much cheaper, and carries no risk of transmitting zoonotic diseases, as it lacks aromatic amino acids such as tryptophan, tyrosine, and phenylalanine. Like collagen, gelatin contains the arginine-glycine-aspartate (RGD) sequence that binds to integrin proteins, allowing for cell attachment. It comprises the repeating amino acid sequence Gly-X-Y, where X and Y are commonly represented by proline and hydroxyproline, respectively. Gelatin is a collagen derivative obtained from the partial hydrolysis of collagen materials upon denaturing the triple helical structure. The composite scaffolds are promising candidates for an acellular skin substitute. Overall, the addition of elastin and CNC improved the properties of gelatin-based scaffolds. HDF cultured on the scaffolds expressed collagen type I and α-SMA proteins, indicating the scaffolds’ biocompatibility with HDF. Chemical analyses revealed that despite chemical and structural alterations, both elastin and CNC were integrated into the gelatin scaffold. Tensile strength analysis revealed that increasing the CNC concentration reduced the scaffolds’ stiffness. Although the group with 0.5% ( w/ v) CNC recorded the highest pore size homogeneity, the diameters of most of the pores in the composite scaffolds ranged from 100 to 200 μm, which is sufficient for cell migration. The composite scaffolds demonstrated higher porosity and swelling capacity and improved enzymatic resistance compared to the controls. The physicochemical and mechanical properties of the scaffolds, and their cellular biocompatibility with human dermal fibroblasts (HDF), were evaluated. The composite scaffolds were composed of different concentrations of CNC, whereas scaffolds made of pure gelatin and a gelatin–elastin mixture served as controls. The scaffolds were fabricated using the freeze-drying method. This study aimed to fabricate and characterise composite scaffolds composed of gelatin, elastin, and cellulose nanocrystals (CNC) and crosslinked with genipin. Hence, gelatin requires crosslinking and reinforcement with other materials. Gelatin usage in scaffold fabrication is limited due to its lack of enzymatic and thermal resistance, as well as its mechanical weakness.
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