Gov Nir S
Department of Chemical Physics, The Weizmann Institute of Science, POB 26, Rehovot, Israel.
Phys Rev E Stat Nonlin Soft Matter Phys. 2008 Jul;78(1 Pt 1):011916. doi: 10.1103/PhysRevE.78.011916. Epub 2008 Jul 24.
The formation of bundles composed of actin filaments and cross-linking proteins is an essential process in the maintenance of the cells' cytoskeleton. It has also been recreated by in-vitro experiments, where actin networks are routinely produced to mimic and study the cellular structures. It has been observed that these bundles seem to have a well-defined width distribution, which has not been adequately described theoretically. We propose here that packing defects of the filaments, quenched and random, contribute an effective repulsion that counters the cross-linking adhesion energy and leads to a well-defined bundle width. This is a two-dimensional strain-field version of the classic Rayleigh instability of charged droplets.
由肌动蛋白丝和交联蛋白组成的束状结构的形成是维持细胞骨架的一个重要过程。这一过程也已通过体外实验得以重现,在这些实验中,肌动蛋白网络被常规性地构建出来以模拟和研究细胞结构。据观察,这些束状结构似乎具有明确的宽度分布,但从理论上尚未得到充分描述。我们在此提出,细丝的淬火和随机堆积缺陷产生了一种有效的排斥力,该排斥力抵消了交联粘附能,并导致了明确的束宽度。这是经典的带电液滴瑞利不稳定性的二维应变场版本。