Actomyosin contractility originating from interactions between F-actin and myosin motors in the actin cytoskeleton generates mechanical forces and drives a wide range of cellular processes including cell migration and cytokinesis. To probe the interactions between F-actin and myosin motors, the myosin motility assay has been popularly employed, which consists of myosin heads attached to a glass surface and F-actins gliding on the surface via interactions with the heads. Several experiments have shown that F-actins move in a collective fashion due to volume-exclusion effects between neighboring F-actins. Furthermore, Computational models have shown how changes in key parameters lead to diverse pattern formation in motility assay. However, in most of the computational models, myosin motors were implicitly considered by applying a constant propulsion force to filaments to reduce computational cost. This simplification limits the physiological relevance of the insights provided by the models and potentially leads to artifacts. In this study, we employed an agent-based computational model for the motility assay with explicit immobile motors interacting with filaments. We rigorously account for the kinetics of myosin motors including the force-velocity relationship for walking and the binding and unbinding behaviors. We probed the effects of the length, rigidity, and concentration of filaments and repulsive strength on collective movements and pattern formation. It was found that four distinct types of structures—homogeneous networks, flocks, bands, and rings—emerged as a result of collisions between gliding filaments. We further analyzed the frequency and morphology of these structures and the curvature, alignment, and rotational motions of filaments. Our study provides better insights into the origin and properties of patterns formed by gliding filaments beyond what was shown before.

中文翻译：

---

运动测定中分子马达驱动的多种模式的出现

肌动球蛋白收缩力源自肌动蛋白细胞骨架中的 F-肌动蛋白和肌球蛋白马达之间的相互作用，产生机械力并驱动广泛的细胞过程，包括细胞迁移和胞质分裂。为了探测 F-肌动蛋白和肌球蛋白马达之间的相互作用，肌球蛋白运动测定已被广泛采用，其由附着在玻璃表面的肌球蛋白头和通过与头的相互作用在表面上滑动的 F-肌动蛋白组成。多项实验表明，由于相邻 F-肌动蛋白之间的体积排斥效应，F-肌动蛋白以集体方式移动。此外，计算模型已经表明关键参数的变化如何导致运动测定中不同模式的形成。然而，在大多数计算模型中，通过向肌丝施加恒定的推进力来隐式考虑肌球蛋白马达，以降低计算成本。这种简化限制了模型提供的见解的生理相关性，并可能导致伪影。在这项研究中，我们采用了基于代理的计算模型来进行运动测定，其中明确的固定电机与细丝相互作用。我们严格地解释了肌球蛋白马达的动力学，包括行走的力-速度关系以及结合和解除结合行为。我们探讨了细丝的长度、硬度和浓度以及排斥强度对集体运动和图案形成的影响。研究发现，滑动细丝之间的碰撞会产生四种不同类型的结构——同质网络、簇、带和环。我们进一步分析了这些结构的频率和形态以及细丝的曲率、排列和旋转运动。我们的研究提供了对滑动细丝形成的图案的起源和特性的更好的见解，超出了之前的研究。