Abstract On-aim control of protein adsorption onto a solid surface remains challenging due to the complex interactions involved in this process. Through computational simulation, it is possible to gain molecular-level mechanistic insight into the movement of proteins at the water–solid interface, which allows better prediction of protein behaviors in adsorption and fouling systems. In this work, a mesoscale coarse-grained simulation method was used to investigate the aggregation and adsorption processes of multiple 12-alanine (12-Ala) hydrophobic peptides onto a gold surface. It was observed that around half (46.6%) of the 12-Ala peptide chains could form aggregates. 30.0% of the individual peptides were rapidly adsorbed onto the solid surface; after a crawling process on the surface, some of these (51.0%) merged into each other or merged with floating peptides to form adsorbed aggregates. The change in the solid–liquid interface due to peptide deposition has a potential influence on the further adsorption of single peptide chains and aggregates in the bulk water. Overall, the findings from this work help to reveal the mechanism of multi-peptide adsorption, and consequentially build a basis for the understanding of multi-protein adsorption onto a solid surface.

中文翻译：

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不带电固体表面的多肽吸附：粗粒度模拟研究

摘要 由于该过程中涉及复杂的相互作用，因此对固体表面上的蛋白质吸附进行目标控制仍然具有挑战性。通过计算模拟，可以在分子水平上深入了解蛋白质在水-固界面处的运动，从而更好地预测吸附和污染系统中的蛋白质行为。在这项工作中，中尺度粗粒度模拟方法用于研究多个 12-丙氨酸 (12-Ala) 疏水肽在金表面上的聚集和吸附过程。据观察，大约一半 (46.6%) 的 12-Ala 肽链可以形成聚集体。30.0% 的单个肽被快速吸附到固体表面；在表面爬行过程之后，其中一些（51. 0%) 相互合并或与浮动肽合并形成吸附聚集体。由于肽沉积引起的固液界面变化对单个肽链和聚集体在大量水中的进一步吸附具有潜在影响。总的来说，这项工作的发现有助于揭示多肽吸附的机制，从而为理解多蛋白质吸附到固体表面上奠定基础。