Structure of a designed protein cage that self-assembles into a highly porous cube.

Structure of a designed protein cage that self-assembles into a highly porous cube.
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DOI:
10.1038/nchem.2107
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发表时间:
2014-12
期刊:
影响因子:
21.8
通讯作者:
--
中科院分区:
化学1区
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--
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天然蛋白质可以成为多聚体、自组装结构的通用构建模块。然而,创建具有特定几何形状和化学性质的基于蛋白质的组装体仍然具有挑战性。高多孔材料代表了设计组装特别有趣的目标。在这里,我们利用一种策略,使用连续的 α 螺旋连接体融合两种天然蛋白质寡聚体,设计一种新型蛋白质,该蛋白质可自组装成 750 kDa、直径 225 Å 的立方体笼,在直径 130 Å 的内腔中具有大开口。笼的晶体结构显示出与设计模型的原子水平一致,而电子显微镜、天然质谱和小角度 X 射线散射揭示了溶液中的替代组装形式。这些研究表明,具有特定形状的大型多孔组件的精确设计是可行的,而进一步的特异性改进可能需要限制选择替代形式的灵活性。这些结果为生物纳米技术、纳米医学和材料科学应用的先进材料的设计奠定了基础。
Natural proteins can be versatile building blocks for multimeric, self-assembling structures. Yet, creating protein-based assemblies with specific geometries and chemical properties remains challenging. Highly porous materials represent particularly interesting targets for designed assembly. Here we utilize a strategy of fusing two natural protein oligomers using a continuous alpha-helical linker to design a novel protein that self assembles into a 750 kDa, 225 Å diameter, cube-shaped cage with large openings into a 130 Å diameter inner cavity. A crystal structure of the cage showed atomic level agreement with the designed model, while electron microscopy, native mass spectrometry, and small angle x-ray scattering revealed alternate assembly forms in solution. These studies show that accurate design of large porous assemblies with specific shapes is feasible, while further specificity improvements will likely require limiting flexibility to select against alternative forms. These results provide a foundation for the design of advanced materials with applications in bionanotechnology, nanomedicine and material sciences.
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