Protein Translocation through a MoS2 Nanopore:A Molecular Dynamics Study
Protein Translocation through a MoS2 Nanopore:A Molecular Dynamics Study
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通过 MoS2 纳米孔的蛋白质易位：分子动力学研究
DOI：
10.1021/acs.jpcc.7b07842
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发表时间：
2018-02-01
影响因子：
3.7
通讯作者：
Zhou, Jian
中科院分区：
文献类型：
--
作者：
Chen, Huang;Li, Libo;Zhou, Jian
单分子蛋白质测序对于广泛的研究和应用领域至关重要，其中最近出现的2D纳米孔开辟了前所未有的可能性。通过2D纳米孔的蛋白质移位在基于纳米孔的分析中起着至关重要的作用，其中可以采用各种检测或测序方法。研究蛋白质在各种2D纳米孔中的移位是至关重要的，这可能有助于设计高效的纳米孔装置。然而，除了石墨烯之外，很少有2D材料在这方面进行了研究。在这项工作中，采用分子动力学（MD）模拟来研究使用MoS 2纳米孔进行单分子蛋白质测序的可行性。苯丙氨酸-甘氨酸重复肽和从硫氧还蛋白蛋白的序列的肽在其扩展的未折叠状态下进行了研究，其自发吸附到MoS 2膜上。这些肽在MoS_2上保持吸附，并通过膜单向渗透。
Single-molecule protein sequencing is essential for a wide range of research and application fields, where the recently emerging 2D nanopores have open unprecedented possibilities. The protein translocating through a 2D nanopore plays vital roles in the nanopore-based analysis, where various detection or sequencing method could be employed. It is critically important to study the protein translocating through various 2D nanopores, which may help design efficient nanopore devices. However, few 2D materials other than graphene have been studied in this context yet. In this work, molecular dynamics (MD) simulations were employed to investigate the feasibility of single-molecule protein sequencing with a MoS2 nanopore. Both phenylalanine–glycine repeat peptides and a peptide with the sequence taken from the thioredoxin protein were studied in their extended unfolded state, which adsorbed onto the MoS2 membrane spontaneously. These peptides kept adsorbing onto MoS2 and permeated unidirectionally through the Mo...