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通过设计的分子间π-π 相互作用实现具有相同构建块的蛋白质纳米笼的各向异性组装。

Shape-Anisotropic Assembly of Protein Nanocages with Identical Building Blocks by Designed Intermolecular π-π Interactions.

机构信息

College of Food Science & Nutritional Engineering, Beijing Key Laboratory of Functional Food from Plant Resources, China Agricultural University, Beijing, 100083, China.

School of Food Science and Technology, National Engineering Research Center of Seafood, Dalian Polytechnic University, Dalian, 116034, China.

出版信息

Adv Sci (Weinh). 2023 Dec;10(35):e2305398. doi: 10.1002/advs.202305398. Epub 2023 Oct 23.

DOI:10.1002/advs.202305398
PMID:37870198
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10724428/
Abstract

Protein lattices that shift the structure and shape anisotropy in response to environmental cues are closely coupled to potential functionality. However, to design and construct shape-anisotropic protein arrays from the same building blocks in response to different external stimuli remains challenging. Here, by a combination of the multiple, symmetric interaction sites on the outer surface of protein nanocages and the tunable features of phenylalanine-phenylalanine interactions, a protein engineering approach is reported to construct a variety of superstructures with shape anisotropy, including 3D cubic, 2D hexagonal layered, and 1D rod-like crystalline protein nanocage arrays by using one single protein building block. Notably, the assembly of these crystalline protein arrays is reversible, which can be tuned by external stimuli (pH and ionic strength). The anisotropic morphologies of the fabricated macroscopic crystals can be correlated with the Å-to-nm scale protein arrangement details by crystallographic elucidation. These results enhance the understanding of the freedom offered by an object's symmetry and inter-object π-π stacking interactions for protein building blocks to assemble into direction- and shape-anisotropic biomaterials.

摘要

蛋白质晶格可以根据环境线索改变结构和形状各向异性,与潜在功能密切相关。然而,设计和构建由相同构建块组成的形状各向异性蛋白质阵列,以响应不同的外部刺激仍然具有挑战性。在这里,通过蛋白质纳米笼外表面上的多个对称相互作用位点和苯丙氨酸-苯丙氨酸相互作用的可调特性的结合,报道了一种蛋白质工程方法,用于构建具有形状各向异性的各种超结构,包括 3D 立方、2D 六方层状和 1D 棒状结晶蛋白质纳米笼阵列,使用单个蛋白质构建块。值得注意的是,这些结晶蛋白质阵列的组装是可逆的,可以通过外部刺激(pH 和离子强度)进行调节。通过晶体学阐明,可以将所制备的宏观晶体的各向异性形态与 Å 到 nm 尺度的蛋白质排列细节相关联。这些结果增强了对物体对称性和对象间π-π堆积相互作用为蛋白质构建块提供的自由度的理解,这些自由度可用于组装具有方向和形状各向异性的生物材料。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc3/10724428/1246bbadda22/ADVS-10-2305398-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc3/10724428/2e77f5aa9929/ADVS-10-2305398-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc3/10724428/0e87b2c77198/ADVS-10-2305398-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc3/10724428/6dfd1911d810/ADVS-10-2305398-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc3/10724428/1246bbadda22/ADVS-10-2305398-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc3/10724428/2e77f5aa9929/ADVS-10-2305398-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc3/10724428/0e87b2c77198/ADVS-10-2305398-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc3/10724428/6dfd1911d810/ADVS-10-2305398-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc3/10724428/1246bbadda22/ADVS-10-2305398-g001.jpg

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Redesign of protein nanocages: the way from 0D, 1D, 2D to 3D assembly.蛋白质纳米笼的再设计:从 0D、1D、2D 到 3D 组装的途径。
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