Collagen Rich Scaffolds for Liver Engineering: A Step Forward to an Artificial Liver

Martin, Catherine Ann; Subathra, R.; Jayanthi, V; Reddy, Srinivas; Varghese, Joy; Rela, Mohammed; Kalkura, Narayana

doi:10.1016/j.jceh.2016.06.144

Cited by 2 publications

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“…The spectrum clearly showed the similar chemical structures between fibroin and gelatin that are characteristic of protein absorption. FTIR spectrum of fibroin comprised of amide I (1640 cm -1 ), indicating the carbonyl (C=O) stretching; amide II (1515 cm -1 ), showing the vibration on the plane of the N-H bond and C-N stretching; amide III (1236 cm -1 ) referring to C-N stretching and N-H deformation, and O-H stretching appearing at 3276 cm -1 [13][14][15]. Likewise, the gelatin spectrum presented the main components of amide I, II, and III with a slight shift of wavelength number.…”

Section: Resultsmentioning

confidence: 99%

“…Therefore, their amino acid and secondary structure were different. The secondary structure of the proteins was estimated thoroughly by the deconvolution and curve fitting of the amide I band [13,16]. The formula ratios of fibroin: gelatin at 8:2 exhibited higher percentages of random coil structure compared to those of fibroin:gelatin at 7:3 and contained less β-sheet.…”

Section: Resultsmentioning

confidence: 99%

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Fabrication, Characterization, and Biocompatibility Study of Gelatin-Blended Fibroin Scaffold

Naksuwan

Chaipayang

Charoeythornkhajhornchai

et al. 2023

ASEAN Sci Tech Rept

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This research investigates the biocompatibility of gelatin-blended fibroin scaffold fabricated by freeze-dry process. The morphology showed interconnected spongy spheres and polygons shapes with a pore size of 14.144 ± 11.31 and 19.4822 ± 18.71 micrometers, respectively. The formula ratio of fibroin: gelatin of 8:2 contained more random coil, while the formula ratio of fibroin: gelatin of 7:3 exhibited more β-sheet structure. The result revealed that gelatin influences fibroin conformational transition from random coil to beta, which might result from better hydrophobic characteristics. The surface of the formula ratio of fibroin: gelatin at 8:2 and 7:3 was 125.88 ± 9.85 and 130.07 ± 3.72 degrees, indicating the formula ratio of fibroin: gelatin at 7:3 had more hydrophobicity than the formula ratio of fibroin: gelatin at 8:2. The biocompatibility of scaffolds was determined for both formulas of human keratinocyte (HaCaT) and African green monkey kidney (Vero) cell lines by MTT assay. The formula ratio of fibroin: gelatin at 8:2 with various concentrations of 62.50, 125, 250, 500, and 1,000 µg/mL had cell viability percentages of 96.31, 101.74, 97.81, 104.15, and 103.22%, respectively. The formula ratio of fibroin: gelatin at 7:3 with various concentrations of 62.50, 125, 250, 500, and 1,000 µg/mL had cell viability percentages of 106.38, 104.28, 108.54, 97.42, and 97.65%, respectively. The growth of cell lines showed better performance with the hydrophilic characteristics of the scaffold, and it did not make it toxic to the HaCaT and Vero cell lines. These results demonstrated the possibility of gelatin-blended scaffold as a supporting material for skin tissue engineering, especially for wound healing.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%