蛋白质空间约束对膜蛋白多面体对称性的影响,Physical Review E

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蛋白质空间约束对膜蛋白多面体对称性的影响
Physical Review E ( IF 2.4 ) Pub Date : 2020-10-23 , DOI: 10.1103/physreve.102.042411
Mingyuan Ma ₁ , Christoph A Haselwandter ₁

Affiliation

实验表明，在水性环境中，脂质和膜蛋白可以自组装成膜蛋白多面体纳米颗粒 (MPPNs)。MPPNs 是封闭的球形囊泡，由脂质双层膜和膜蛋白组成，膜蛋白呈多面体排列。观察到的 MPPNs 的对称性和大小可以从 MPPNs 中蛋白质诱导的脂质双层变形、MPPNs 球形所需的蛋白质堆积拓扑缺陷以及 MPPN 自组装中的热波动之间的相互作用来理解。我们在这里探索蛋白质空间约束对 MPPN 形状的影响。这里考虑的蛋白质空间约束可能来自膜外蛋白质结构域的明确形状，膜外具有柔性结构域的膜蛋白之间的熵排斥，或其他分子与膜蛋白的结合。计算蛋白质空间约束下的 MPPN 自组装图，我们发现蛋白质空间约束可以强烈影响 MPPN 自组装。根据所考虑的具体情况，蛋白质空间约束可能会使 MPPN 自组装图的大部分没有明确定义的 MPPN 对称性或显着扩展由高度对称 MPPN 状态主导的 MPPN 自组装图的区域，例如具有二十面体的 MPPN或怠慢立方体对称性。我们的结果表明，蛋白质空间约束的修饰可能允许具有特定对称性、大小和蛋白质组成的 MPPN 的定向自组装，从而可能有助于进一步利用 MPPN 进行膜蛋白结构分析或靶向药物递送。

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Effect of protein steric constraints on the symmetry of membrane protein polyhedra

Experiments have shown that, in an aqueous environment, lipids and membrane proteins can self-assemble into membrane protein polyhedral nanoparticles (MPPNs). MPPNs are closed, spherical vesicles composed of a lipid bilayer membrane and membrane proteins, with a polyhedral arrangement of membrane proteins. The observed symmetry and size of MPPNs can be understood from the interplay of protein-induced lipid bilayer deformations in MPPNs, topological defects in protein packing necessitated by the spherical shape of MPPNs, and thermal fluctuations in MPPN self-assembly. We explore here the effect of protein steric constraints on MPPN shape. The protein steric constraints considered here may arise from a well-defined shape of protein domains outside the membrane, entropic repulsion between membrane proteins with flexible domains outside the membrane, or binding of other molecules to membrane proteins. Calculating MPPN self-assembly diagrams under protein steric constraints we find that protein steric constraints can strongly affect MPPN self-assembly. Depending on the specific scenario considered, protein steric constraints can leave large portions of the MPPN self-assembly diagrams with no clearly defined MPPN symmetry or substantially expand the regions of MPPN self-assembly diagrams dominated by highly symmetric MPPN states, such as MPPNs with icosahedral or snub cube symmetry. Our results suggest that modification of protein steric constraints may allow the directed self-assembly of MPPNs with specified symmetry, size, and protein composition and may thus facilitate the further utilization of MPPNs for membrane protein structural analysis or targeted drug delivery.

更新日期：2020-10-30

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