Inverse design of triblock Janus spheres for self-assembly of complex structures in the crystallization slot via digital alchemy
Inverse design of triblock Janus spheres for self-assembly of complex structures in the crystallization slot via digital alchemy
复制标题
通过数字炼金术在结晶槽中自组装复杂结构的三嵌段Janus球的逆向设计
DOI：
10.1039/d2sm01593e
复制
发表时间：
2023
期刊：
影响因子：
3.4
通讯作者：
Glotzer, Sharon C.
中科院分区：
文献类型：
--
作者：
Rivera-Rivera, Luis Y.;Moore, Timothy C.;Glotzer, Sharon C.
数字炼金术框架是一种扩展的集成模拟技术，它将粒子属性作为热力学变量，使胶体粒子的逆设计能够实现所需的行为。在这里，我们扩展了数字炼金术框架，用于自组装成目标晶体结构的斑块球体的逆向设计。为了将势能约束为非平凡解，我们进行了常数次维里系数的数字炼金术模拟。我们优化了模型三块Janus球体中斑块相互作用的大小、范围和强度，以实现二维kagome和snub方形晶格以及三维焦绿石晶格的自组装，并利用所设计的模型演示了这三种目标结构的自组装。为kagome和snub方形晶格设计的颗粒组装成目标结构的高质量簇，而来自类似多晶体的竞争降低了焦绿石组装的收率。我们发现炼金术设计的势并不总是与物理直觉相匹配，说明该方法能够找到优化问题的非平凡解。我们确定了导致目标结构自组装的第二维里系数窗口，类似于蛋白质结晶中的结晶槽。
The digital alchemy framework is an extended ensemble simulation technique that incorporates particle attributes as thermodynamic variables, enabling the inverse design of colloidal particles for desired behavior. Here, we extend the digital alchemy framework for the inverse design of patchy spheres that self-assemble into target crystal structures. To constrain the potentials to non-trivial solutions, we conduct digital alchemy simulations with constant second virial coefficient. We optimize the size, range, and strength of patchy interactions in model triblock Janus spheres to self-assemble the 2D kagome and snub square lattices and the 3D pyrochlore lattice, and demonstrate self-assembly of all three target structures with the designed models. The particles designed for the kagome and snub square lattices assemble into high quality clusters of their target structures, while competition from similar polymorphs lower the yield of the pyrochlore assemblies. We find that the alchemically designed potentials do not always match physical intuition, illustrating the ability of the method to find nontrivial solutions to the optimization problem. We identify a window of second virial coefficients that result in self-assembly of the target structures, analogous to the crystallization slot in protein crystallization.