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The Role Of Dialysis And Freezing On Structural Conformation, Thermal Properties And Morphology Of Silk Fibroin Hydrogels

机译:透析和冻结对丝素蛋白水凝胶的结构形态,热学性质和形态的影响

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摘要

Silk fibroin has been widely explored for many biomedical applications, due to its biocompatibility and biodegradability. The aim of this work was to study the role of dialysis and freezing on structural conformation, thermal properties and morphology of silk fibroin hydrogels. Hydrogels were prepared after 3 and 7 days of dialysis and the effect of freezing was analyzed. For that purpose, a part of the fibroin hydrogels underwent freezing at -20 °C for 24 h, followed by lyophilization and the rest of the hydrogels were kept at 8 °C for 24 h, with further lyophilization. The fibroin hydrogels were characterized by X-ray diffraction (XRD), Fourier transformed infrared spectroscopy (FTIR), thermogravimetric analysis (TGA) and scanning electron microscopy (SEM). Measurements by XRD and FTIR indicated that silk I and silk II structures were present in the fibroin hydrogels and that the secondary structure of fibroin is transformed mostly to β-sheet during the gelation process. Thermal analysis indicated that fibroin hydrogels are thermally stable with the degradation peak at around 330-340 °C. SEM micrographs showed porous structures and the fibroin hydrogels subjected to freezing presented a much larger pore size. Results indicate that the dialysis time and freezing did not alter the material crystallinity, conformation or thermal behavior; however, hydrogel microstructure was strongly affected by dialysis time and freezing, showing controlled pores size. This study provides fundamental knowledge on silk fibroin hydrogels preparation and properties and the studied hydrogels are promising to be used in the biomaterial field.
机译:丝素蛋白因其生物相容性和生物降解性而在许多生物医学应用中得到了广泛的探索。这项工作的目的是研究透析和冷冻对丝素蛋白水凝胶的结构构象,热学性质和形态的作用。在透析3天和7天后制备水凝胶,并分析冷冻作用。为此目的,将一部分纤维蛋白水凝胶在-20°C下冷冻24 h,然后冻干,将其余的水凝胶在8°C下保持24 h,然后进一步冻干。纤维蛋白水凝胶的特征在于X射线衍射(XRD),傅立叶变换红外光谱(FTIR),热重分析(TGA)和扫描电子显微镜(SEM)。通过XRD和FTIR的测量表明,丝蛋白I和丝II结构存在于丝蛋白水凝胶中,并且丝蛋白的二级结构在胶凝过程中大部分转化为β-片层。热分析表明,丝心蛋白水凝胶是热稳定的,降解峰在330-340°C左右。 SEM显微照片显示出多孔结构,并且经受冷冻的丝蛋白水凝胶呈现出大得多的孔径。结果表明,透析时间和冷冻不会改变材料的结晶度,构象或热行为。然而,水凝胶的微结构受透析时间和冷冻的强烈影响,显示出可控制的孔尺寸。该研究提供了关于丝素蛋白水凝胶的制备和性质的基础知识,并且所研究的水凝胶有望用于生物材料领域。

著录项

  • 作者

    Ribeiro M.;

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  • 年度 2015
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  • 原文格式 PDF
  • 正文语种 eng
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