Controlling viral capsid assembly with templating
Controlling viral capsid assembly with templating
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DOI：
10.1103/physreve.77.051904
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发表时间：
2008-05-01
影响因子：
2.4
通讯作者：
Hagan, Michael F.
中科院分区：
文献类型：
--
作者：
Hagan, Michael F.
我们开发了粗粒度的模型，描述了功能化的纳米粒子的病毒衣壳蛋白的动态包埋。我们发现，蛋白质亚基和纳米颗粒之间的某些形式的合作相互作用可以显着提高组装的速率和鲁棒性，相比于自发组装成空衣壳的亚基。对于大的核心-亚基相互作用，亚基以无序的方式吸附在核心表面上，然后进行合作重排成有序的衣壳结构。这些组装途径与空衣壳形成所鉴定的任何途径不同。我们的模型可以直接应用于最近的实验，其中病毒衣壳蛋白围绕功能化的无机纳米颗粒组装[Sun等人，Proc. Natl. Acad. Sci. U.S.A. 104，1354（2007）]。此外，我们还讨论了更广泛的影响，了解病毒复制过程中的单链基因组分子的动态crossidation和开发多组分纳米结构材料。
We develop coarse-grained models that describe the dynamic encapsidation of functionalized nanoparticles by viral capsid proteins. We find that some forms of cooperative interactions between protein subunits and nanoparticles can dramatically enhance rates and robustness of assembly, as compared to the spontaneous assembly of subunits into empty capsids. For large core-subunit interactions, subunits adsorb onto core surfaces en masse in a disordered manner, and then undergo a cooperative rearrangement into an ordered capsid structure. These assembly pathways are unlike any identified for empty capsid formation. Our models can be directly applied to recent experiments in which viral capsid proteins assemble around functionalized inorganic nanoparticles [Sun et al., Proc. Natl. Acad. Sci. U.S.A. 104, 1354 (2007)]. In addition, we discuss broader implications for understanding the dynamic encapsidation of single-stranded genomic molecules during viral replication and for developing multicomponent nanostructured materials.