Higher-Order VLP-Based Protein Macromolecular Framework Structures Assembled via Coiled-Coil Interactions
Higher-Order VLP-Based Protein Macromolecular Framework Structures Assembled via Coiled-Coil Interactions
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DOI：
10.1021/acs.biomac.3c00410
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发表时间：
2023-07-19
影响因子：
6.2
通讯作者：
Douglas，Trevor
中科院分区：
文献类型：
--
作者：
Hewagama，Nathasha D.;Uchida，Masaki;Douglas，Trevor
等级组织是在生物系统中观察到的允许高效和有效运作的基本特征之一。病毒样颗粒(VLP)是分级组织的超分子结构的典范，其中许多亚单位自组装产生功能笼状结构。利用VLP构建二维和三维高阶结构是仿生功能材料发展的一个新兴研究领域。来源于P22噬菌体的VLP可以通过几种技术包裹酶和模块单元来构建更高阶的催化材料，从而重新用作纳米反应器。在本研究中，我们使用盘绕多肽相互作用将P22颗粒间组装介导成高度稳定的无定形蛋白质大分子框架(PMF)材料，其中组装不依赖于VLP形态，这是以前报道的P22 PMF组装中观察到的限制。许多被包裹的酶在P22 VLP形态转变所需的苛刻条件下失去了最佳的功能。因此，基于盘绕线圈的PMF为构建与敏感酶相容的功能性高阶催化材料提供了一个合适且通用的平台。我们表征了PMF的材料性质，并利用无序的PMF构建了一种生物催化的3D材料，进行了单步和多步催化。
Hierarchical organization is one of the fundamental features observed in biological systems that allows for efficient and effective functioning. Virus-like particles (VLPs) are elegant examples of a hierarchically organized supramolecular structure, where many subunits are self-assembled to generate the functional cage-like architecture. Utilizing VLPs as building blocks to construct two- and three-dimensional (3D) higher-order structures is an emerging research area in developing functional biomimetic materials. VLPs derived from P22 bacteriophages can be repurposed as nanoreactors by encapsulating enzymes and modular units to build higher-order catalytic materials via several techniques. In this study, we have used coiled-coil peptide interactions to mediate the P22 interparticle assembly into a highly stable, amorphous protein macromolecular framework (PMF) material, where the assembly does not depend on the VLP morphology, a limitation observed in previously reported P22 PMF assemblies. Many encapsulated enzymes lose their optimum functionalities under the harsh conditions that are required for the P22 VLP morphology transitions. Therefore, the coiled-coil-based PMF provides a fitting and versatile platform for constructing functional higher-order catalytic materials compatible with sensitive enzymes. We have characterized the material properties of the PMF and utilized the disordered PMF to construct a biocatalytic 3D material performing single- and multistep catalysis.