The Effect of Protein Fusions on the Production and Mechanical Properties of Protein-Based Materials
The Effect of Protein Fusions on the Production and Mechanical Properties of Protein-Based Materials
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蛋白质融合对蛋白质基材料的生产和机械性能的影响
DOI：
10.1002/adfm.201402997
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发表时间：
2015
影响因子：
19
通讯作者：
Bondos, Sarah E.
中科院分区：
文献类型：
--
作者：
Tsai, Shang-Pu;Howell, David W.;Huang, Zhao;Hsiao, Hao-Ching;Lu, Yang;Matthews, Kathleen S.;Lou, Jun;Bondos, Sarah E.
蛋白质实现了生物体的大多数重要分子功能，包括结构支持，能量产生，生物分子传感，化学催化，储存和降解。虽然捕获材料中的蛋白质可以创建模拟这些功能的设备，但由于蛋白质结构对化学环境的敏感性，这一过程具有挑战性。使用重组DNA方法，可以通过融合编码自组装蛋白的基因和所需的功能蛋白来掺入特定功能，以产生自组装成功能化材料的单一多肽。然而，功能性蛋白质具有破坏蛋白质产生、蛋白质组装和/或所得材料的结构和机械性质的潜力。24种融合蛋白是基于Ultrabithorax创建的，Ultrabithorax是一种果蝇转录因子，可以在体外自组装成材料。附加的蛋白质决定了相应蛋白质融合物的溶解度和纯化产率。溶解度和产率的任何损失都可以通过融合高度可溶的第三种蛋白质来减轻。所有蛋白质融合体都能同样好地自组装，产生具有相似形态的材料。将增强型绿色荧光蛋白融合到Ultrabithorax上会影响所得纤维的机械性能。得出的结论是，比最初预期的更广泛的蛋白质可以成功地结合到弹性蛋白质基材料中。
Proteins implement most of the vital molecular functions of living organisms, including structural support, energy generation, biomolecule sensing, and chemical catalysis, storage, and degradation. While capturing proteins in materials could create devices that mimic these functions, this process is challenging due to the sensitivity of protein structure to the chemical environment. Using recombinant DNA methods, specific functions can be incorporated by fusing the gene encoding a self‐assembling protein and the desired functional protein, to produce a single polypeptide that self‐assembles into functionalized materials. However, the functional protein has the potential to disrupt protein production, protein assembly, and/or the structure and mechanical properties of the resulting materials. 24 fusion proteins are created based on Ultrabithorax, aDrosophilatranscription factor that self‐assembles into materials in vitro. The appended proteins dictate the solubility and purification yield of the corresponding protein fusions. Any loss of solubility and yield can be mitigated by fusing a third protein that is highly soluble. All protein fusions self‐assemble equally well to produce materials with similar morphologies. Fusing enhanced green fluorescent protein to Ultrabithorax influences mechanical properties of the resulting fibers. It is concluded that a far wider range of proteins can be successfully incorporated into elastomeric protein‐based materials than originally anticipated.