Effect of β-sheet crystals on the thermal and rheological behavior of protein-based hydrogels derived from gelatin and silk fibroin
Effect of β-sheet crystals on the thermal and rheological behavior of protein-based hydrogels derived from gelatin and silk fibroin
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DOI：
10.1002/mabi.200500076
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发表时间：
2005-08-12
影响因子：
4.6
通讯作者：
Hudson, SM
中科院分区：
文献类型：
--
作者：
Gil, ES;Spontak, RJ;Hudson, SM
通过将明胶 (G) 与无定形家蚕丝素蛋白 (SF) 混合，随后在暴露于甲醇或甲醇/水溶液时促进 SF 中 β-折叠晶体的形成，制备了新型蛋白质水凝胶。所得水凝胶的差示扫描量热法证实了高 G 浓度下环境温度和体温之间 G 螺旋-螺旋转变的存在和热可逆性。在低 G 浓度下，这种转变会转移到更高的温度，并且逐渐变得不那么明显。补充动态流变学测量揭示了在形成 β-折叠晶体之前，共混物中 G 螺旋-螺旋转变温度通常在 30 至 36 摄氏度之间的固液交叉。在 SF 中引入 β-折叠构象可以稳定水凝胶网络，并将水凝胶的类固体行为扩展到体温以上的高温，SE 释放量低至 10 wt.-%。混合明胶/丝素蛋白水凝胶中明胶的热可逆螺旋-螺旋构象转变。
Novel protein-based hydrogels have been prepared by blending gelatin (G) with amorphous Bombyx mori silk fibroin (SF) and subsequently promoting the formation of beta-sheet crystals in SF upon exposure to methanol or methanol/water solutions. Differential scanning calorimetry of the resultant hydrogels confirms the presence and thermoreversibility of the G helix-coil transition between ambient and body temperature at high G concentrations. At low G concentrations, this transition is shifted to higher temperatures and becomes progressively less pronounced. Complementary dynamic rheological measurements reveal solid-liquid crossover at the G helix-coil transition temperature typically between 30 and 36 degrees C in blends prior to the formation of beta-sheet crystals. Introducing the beta-sheet conformation in SF stabilizes the hydrogel network and extends the solid-like behavior of the hydrogels to elevated temperatures beyond body temperature with as little as 10 wt.-% SE release. Thermally reversible helix-coil conformational transition of gelatin in mixed gelatin/silk fibroin hydrogels.