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束状肌动蛋白丝网格结构的定量分析。

Quantification of the mesh structure of bundled actin filaments.

机构信息

UT Austin Department of Physics, 2515 Speedway, Austin, Texas, USA.

出版信息

Soft Matter. 2021 May 19;17(19):5034-5043. doi: 10.1039/d1sm00428j.

Abstract

Biopolymer networks are essential for a wide variety of cellular functions. The biopolymer actin is known to self-assemble into a variety of spatial structures in response to physiological and physical mechanisms. So far, the mechanics of networks of single actin filaments and bundles has previously been described. However, the spatial structure of actin bundles remains poorly understood. Here, we investigate this question by bundling actin filaments with systematically varied concentrations of known physical bundling agents (MgCl2 and PEG) and physiological bundling agents (α-actinin and fascin). We image bundled actin networks with confocal microscopy and perform analysis to describe their mesh size and the nearest-distance distribution, which we call "mesh structure". We find that the mesh size ξ scales universally with actin concentration as ξ ∼ [actin]-1/2. However, the dependence of ξ on the concentration of the bundling agent depends on the agent used. Finally, we find that nearest-distance distributions are best fit by Weibull and Gamma distributions. A complete understanding of the mesh structure of biopolymer networks leads to a more mechanistic understanding of the structure of the cytoskeleton, and can be exploited to design filters with variable porosity for microfluidic devices.

摘要

生物聚合物网络对于各种细胞功能至关重要。生物聚合物肌动蛋白已知会根据生理和物理机制自组装成各种空间结构。到目前为止,已经描述了单根肌动蛋白丝和束的网络的力学性质。然而,肌动蛋白束的空间结构仍然知之甚少。在这里,我们通过用已知的物理成束剂(MgCl2 和 PEG)和生理成束剂(α-辅肌动蛋白和细丝蛋白)有系统地改变浓度来捆绑肌动蛋白丝来研究这个问题。我们使用共焦显微镜对捆绑的肌动蛋白网络进行成像,并进行分析以描述它们的网格大小和最近距离分布,我们称之为“网格结构”。我们发现网格大小 ξ 与肌动蛋白浓度普遍成比例,即 ξ∼[肌动蛋白]-1/2。然而, ξ 对成束剂浓度的依赖性取决于所使用的成束剂。最后,我们发现最近距离分布最适合 Weibull 和 Gamma 分布。对生物聚合物网络网格结构的全面理解可以更深入地了解细胞骨架的结构,并可用于设计用于微流控设备的具有可变孔隙率的过滤器。

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