Effect of heat treatment on the structural and conformational changes of regenerated Antheraea pernyi silk fibroin films

Abstract

Regenerated Antheraea pernyi silk fibroin films prepared from calcium nitrate solution were treated with heat for crystallization. The structural and conformational changes caused by heat treatment were investigated with X‐ray diffraction, infrared spectroscopy, and differential scanning calorimetry. The temperature and treatment time of heat greatly influenced the conformation of the regenerated films. The conformational change was caused by heat treatment over 230°C, and the transition was enhanced by increasing time and temperature. The contents of α‐helix, β‐sheet, and random‐coil conformations were calculated and examined to investigate the effect of heat treatment on the conformational changes. The β‐sheet structure could be transformed from a random‐coil conformation on heat treatment, whereas the content of α‐helix structure was nearly unchanged, regardless of heat‐treatment conditions. © 2001 John Wiley & Sons, Inc. J Appl Polym Sci 81: 2271–2276, 2001

Enzymatic degradation of Antheraea pernyi silk fibroin 3D scaffolds and fibers

“…In contrast, the natural Ap-SF fiber containing moreˇ-sheet structures has long-term degradation characteristics. It has been reported that the molecular conformation of the Ap-SF materials changes after treatment with methanol solution, ethanol and other organic solvents and changes with temperature [6][7][8][9]. These observations will allow us to adjust the molecular conformation of Ap-SF based biomaterials which would be applied in tissue engineering or tissue inducing, and to control the biodegradation rates, so as to satisfy numerous tissue regeneration requirements.…”

“…The amino bands of the FT-IR spectra are known to be sensitive to the molecular conformation of Ap-SF [7,14,15]. As shown in Fig.…”

“…The results indicated that the regenerated Ap-SF, like B. mori silk fibroin and collagen, can support hBMSCs attachment, growth and phenotypic maintenance, and has better biocompatibilities for hBMSCs in vitro culture. Based on these features, interest has arisen into the use of Ap-SF as a starting material for advanced biomedical applications such as cell culture substrates, surgical mending materials and tissue engineering scaffolds [5][6][7][8].…”

Structure and properties of regenerated Antheraea pernyi silk fibroin filaments

“…X-ray diffraction patterns of APSF have been provided in earlier reports. 9,13,17,18 According to the results of these reports, the diffraction peaks at 16.4 (lattice spacing d ¼ 5.40 Å ), 16.8 (5.27 Å ), 20.1 (4.41 Å ), and 20.3 (4.37 Å ) belong to the b-sheet structure, and that at 24.1 (3.69 Å ) belongs to the ahelix structure. On the basis of these data, Figure 6 shows that the crystalline component of the native and regenerated APSF filaments mainly consisted of b sheets but had a few a helices.…”

Investigate the Effect of Thawing Process on the Self-Assembly of Silk Protein for Tissue Applications

“…There were several studies focusing on the effect of temperature in different phases of fabrication on silk protein self-assembly [13]. For example, Kweon et al showed that heat treatment on silk-based films could induce secondary conformation transformation [14]. The group of Putthanarat [15] and Zhong [16] pointed out that the drying and incubation temperature had a notable effect on the morphology of silk fibroin nanostructures.…”