Behavior of Protein-Inspired Synthetic Random Heteropolymers
Behavior of Protein-Inspired Synthetic Random Heteropolymers
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DOI：
10.1021/acs.macromol.0c01886
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发表时间：
2020-11-10
期刊：
影响因子：
5.5
通讯作者：
Alexander-Katz, Alfredo
中科院分区：
文献类型：
--
作者：
Hilburg, Shayna L.;Ruan, Zhiyuan;Alexander-Katz, Alfredo
随机杂多聚合物（RHPs）是一类有趣的材料，在许多理论和应用中都很有用。虽然以前的研究通常集中在简化的RHP系统上，但在这里，我们探索了一个更复杂的场景，受到蛋白质等高度异质分子的启发。我们的系统由四种单体组成，模拟不同种类的氨基酸。利用分子动力学模拟和小角度x射线散射，我们探索了这些RHPs在溶液中的动力学和结构特征。我们的研究结果表明，RHPs与异质界面组装，使人联想到蛋白质表面。聚合物骨架在室温下，在纳米到微秒的时间尺度上表现为凝固的熔融球状形态，尽管它们的构象空间对于给定序列具有多个亚稳构象，与内在无序的蛋白质进行比较。局部连通性和化学也被证明对聚合物溶剂化有重大影响。这里提出的工作表明，RHPs与在仿生和生物启发应用中利用的蛋白质有相似之处。
Random heteropolymers (RHPs) are an interesting class of materials useful in many theories and applications. While previous studies typically focused on simplified RHP systems, here we explore a more complex scenario inspired by highly heterogeneous molecules like proteins. Our system consists of four monomers mimicking different classes of amino acids. Using molecular dynamics simulations and small-angle X-ray scattering, we explore dynamical and structural features of these RHPs in solution. Our results show that the RHPs assemble with heterogeneous interfaces reminiscent of protein surfaces. The polymer backbones appear frozen at room temperature on the nano- to microsecond timescale with a molten globule morphology, albeit their conformational space has multiple metastable conformations for a given sequence, drawing comparison to intrinsically disordered proteins. Local connectivity and chemistry are also shown to have a substantial impact on polymer solvation. The work presented here indicates that RHPs share similarities with proteins to be leveraged in biomimetic and bioinspired applications.