Zoccola Marina, Aluigi Annalisa, Vineis Claudia, Tonin Claudio, Ferrero Franco, Piacentino Marco G
National Research Council, Institute for Macromolecular Studies, 13900 Biella (BI), Italy.
Biomacromolecules. 2008 Oct;9(10):2819-25. doi: 10.1021/bm800579a. Epub 2008 Sep 18.
Keratin regenerated from wool and fibroin regenerated from silk were mixed in different proportions using formic acid as the common solvent. Both solutions were cast to obtain films and electrospun to produce nanofibers. Scanning electron microscopy investigation showed that, for all electrospun blends (except for 100% keratin where bead defects are present), the fiber diameter of the mats ranged from 900 (pure fibroin) to 160 nm (pure keratin). FTIR and DSC analysis showed that the secondary structure of the proteins was influenced by the blend ratios and the process used (casting or electrospinning). Prevalence of beta-sheet supramolecular structures was observed in the films, while proteins assembled in alpha-helix/random coil structures were observed in nanofibers. Higher solution viscosity, thinner filaments, and differences in the thermal and structural properties were observed for the 50/50 blend because of the enhanced interactions between the proteins.
以甲酸作为共同溶剂，将从羊毛再生的角蛋白和从丝绸再生的丝素蛋白按不同比例混合。将两种溶液浇铸以获得薄膜，并通过静电纺丝制备纳米纤维。扫描电子显微镜研究表明，对于所有静电纺丝共混物（除了存在珠状缺陷的100%角蛋白），毡垫的纤维直径范围为900nm（纯丝素蛋白）至160nm（纯角蛋白）。傅里叶变换红外光谱（FTIR）和差示扫描量热法（DSC）分析表明，蛋白质的二级结构受共混比例和所用工艺（浇铸或静电纺丝）的影响。在薄膜中观察到β-折叠超分子结构占主导，而在纳米纤维中观察到蛋白质组装成α-螺旋/无规卷曲结构。由于蛋白质之间相互作用增强，对于50/50共混物观察到更高的溶液粘度、更细的细丝以及热性能和结构性能的差异。
