The recombinant spider silk protein eADF4(C16) was genetically fused either with esterase 2 (EST2) or green fluorescent protein (GFP). The fusions EST-eADF4(C16) and GFP-eADF4(C16) were spectroscopically investigated and showed native structures of EST and GFP. The structural integrity was confirmed by the enzymatic activity of EST and the fluorescence of GFP. The spider silk moiety retained its intrinsically unstructured conformation in solution and the self-assembly into either nanofibrils or nanoparticles could be controlled by the concentration of phosphate. Particles, however, showed significantly lower activity of the EST and GFP domains likely caused by a steric hindrance. However, upon self-assembly of EST-eADF4(C16) and GFP-eADF4(C16) into fibrils the protein activities were retained. In general, the fusion of globular enzymes with the spider silk domain allows the generation of fibrous biomaterials with catalytic or light emitting properties.

中文翻译：

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包含酶和荧光活性的蜘蛛丝融合蛋白的自组装

重组蜘蛛丝蛋白eADF4（C16）与酯酶2（EST2）或绿色荧光蛋白（GFP）遗传融合。对融合体EST-eADF4（C16）和GFP-eADF4（C16）进行了光谱研究，显示出EST和GFP的天然结构。通过EST的酶促活性和GFP的荧光证实了结构的完整性。蜘蛛丝部分在溶液中保留了其固有的非结构化构象，并且可以通过磷酸盐的浓度控制自组装成纳米原纤维或纳米颗粒。然而，粒子显示出可能由空间位阻引起的EST和GFP结构域的活性显着降低。然而，自组装的EST-eADF4（C16）和GFP-eADF4（C16）成原纤维后，蛋白活性得以保留。一般来说，