The Fabrication of Gelatin–Elastin–Nanocellulose Composite Bioscaffold as a Potential Acellular Skin Substitute

Abstract

Gelatin usage in scaffold fabrication is limited due to its lack of enzymatic and thermal resistance, as well as its mechanical weakness. Hence, gelatin requires crosslinking and reinforcement with other materials. This study aimed to fabricate and characterise composite scaffolds composed of gelatin, elastin, and cellulose nanocrystals (CNC) and crosslinked with genipin. The scaffolds were fabricated using the freeze-drying method. 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 physicochemical and mechanical properties of the scaffolds, and their cellular biocompatibility with human dermal fibroblasts (HDF), were evaluated. The composite scaffolds demonstrated higher porosity and swelling capacity and improved enzymatic resistance compared to the controls. 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. Tensile strength analysis revealed that increasing the CNC concentration reduced the scaffolds’ stiffness. Chemical analyses revealed that despite chemical and structural alterations, both elastin and CNC were integrated into the gelatin scaffold. HDF cultured on the scaffolds expressed collagen type I and α-SMA proteins, indicating the scaffolds’ biocompatibility with HDF. Overall, the addition of elastin and CNC improved the properties of gelatin-based scaffolds. The composite scaffolds are promising candidates for an acellular skin substitute.

Development and In Vitro Analysis of Layer-by-Layer Assembled Membranes for Potential Wound Dressing: Electrospun Curcumin/Gelatin as Middle Layer and Gentamicin/Polyvinyl Alcohol as Outer Layers

“…The infrared spectrum of curcumin-loaded gelatin showed that the characteristic peak wavelength of gelatin is the absorption bands of amide I (C=O; C–N) at 1641 cm −1 ( Figure 1 c), amide II (N–H) at 1536 cm −1 , and amide III (C=N) at 1240 cm −1 [ 20 ]. The characteristic peak wavelength of curcumin showed that the absorption band of C=C is at 1510 cm −1 , the band of aromatic C–O is at 1283 cm −1 , and the band of C–O–C is at 1154 cm −1 .…”

Underused Marine Resources: Sudden Properties of Cod Skin Gelatin Gel

“…This leads to deterioration in the gelling ability of fish gelatin, a decrease in gelation and melting temperatures, a decrease in gel strength [23][24][25], and increased consumption of gelatin as a food component for hydrogel formation. Many studies have been devoted to finding ways to eliminate these serious disadvantages by treating fish gelatin with various physical, enzymatic, and natural cross-linking agents [26][27][28][29][30][31]; irradiation in various frequency ranges [32,33]; high pressure [34]; enzymatic modification [35][36][37]; and additions of mono-and disaccharides [38,39]. However, the most effective and common way to improve gelling ability and rheological characteristics are the modification of fish gelatin with natural polysaccharides [40][41][42][43].…”