自组装
超分子化学
非共价相互作用
蛋白质结晶
堆积
结晶学
组氨酸
材料科学
超分子组装
晶体工程
纳米技术
化学
化学物理
晶体结构
结晶
氢键
分子
有机化学
生物化学
氨基酸
作者
Mingming Du,Kun Zhou,Runze Yu,Yufeng Zhai,Gang Chen,Qiangbin Wang
出处
期刊:Nano Letters
[American Chemical Society]
日期:2021-02-08
卷期号:21 (4): 1749-1757
被引量:12
标识
DOI:10.1021/acs.nanolett.0c04587
摘要
Engineering noncovalent interactions for assembling nonspherical proteins into supramolecular architectures with tunable morphologies and dynamics is challenging due to the structural heterogeneity and complexity of protein surfaces. Herein, we employed an anisotropic building block l-rhamnulose-1-phosphate aldolase (RhuA) to control supramolecular polymorphism in highly ordered protein assemblies by introducing histidine residues. Histidine-based π–π stacking interactions enabled thermodynamically controlled self-organization of RhuA to form three-dimensional (3D) nanoribbons and crystals. Self-assembly of different 3D crystal phases was kinetically modulated by the strong metal ion-histidine chelation, and double-helical protein superstructures were formed by engineering increased histidine interactions at the RhuA binding surface. Their structural properties and dynamics were determined via fluorescence microscopy, transmission electron microscopy, atomic force microscopy, and small-angle X-ray scattering. This work is aimed at expanding the toolbox for the programming of tunable, highly ordered, protein superstructures and increasing the understanding of the mechanisms of protein interfacial interactions.
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