With the development of various nanomaterial expected to be used in biomedical fields, it is more important to evaluate and understand their potential effects on biological system. In this work, two proteins with different structure, Villin Headpiece (HP35) with α‐helix structure and protofibrils Aβ1‐42 with five β‐strand chains, were selected and their interactions with silicene were studied by means of molecular dynamics (MD) simulation to reveal the potential effect of silicene on the structure and function of biomolecules. The obtained results indicated that silicene could rapidly attract HP35 and Aβ1‐42 fibrils onto the surface to form a stable binding. The adsorption strength was moderate and no significant structural distortion of HP35 and Aβ1‐42 fibrils was observed. Moreover, the strength of calculated the H‐bonds in neighbor chain of Aβ1‐42 fibrils indicated that the mild interactions between silicene and fibrils could regularize the structure of Aβ1‐42 fibrils and stabilize the interactions between five chains of fibrils protein, which might enhance the aggregation of Aβ1‐42 fibrils. This study provides a new insight for understanding the interaction between nanomaterials and biomolecules and moves forward the development of silicene into biomedical fields.

中文翻译：

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通过分子动力学模拟探索硅烯单分子层对绒毛蛋白头饰和淀粉样蛋白原纤维结构和功能的影响。

随着各种纳米材料有望用于生物医学领域的发展，评估和了解它们对生物系统的潜在影响变得更加重要。在这项工作中，选择了两种不同结构的蛋白质，即具有 α-螺旋结构的 Villin Headpiece (HP35) 和具有 5 个 β-链的原纤维 Aβ1-42，并通过分子动力学 (MD) 模拟研究了它们与硅烯的相互作用。揭示硅烯对生物分子结构和功能的潜在影响。结果表明，硅烯可以迅速将HP35和Aβ1-42原纤维吸引到表面上形成稳定的结合。吸附强度适中，没有观察到 HP35 和 Aβ1-42 原纤维的显着结构变形。而且，计算 Aβ1-42 原纤维相邻链中 H 键的强度表明，硅烯和原纤维之间的温和相互作用可以规范 Aβ1-42 原纤维的结构并稳定原纤维蛋白 5 条链之间的相互作用，这可能会增强聚集Aβ1-42 原纤维。该研究为理解纳米材料与生物分子之间的相互作用提供了新的视角，推动了硅烯在生物医学领域的发展。