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在各向同性-向列相转变过程中,F-肌动蛋白溶液的抗衡离子依赖性微观流变学性质。

Counterion-dependent microrheological properties of F-actin solutions across the isotropic-nematic phase transition.

作者信息

He Jun, Mak Michael, Liu Yifeng, Tang Jay X

机构信息

Department of Physics, Brown University, Providence, Rhode Island 02912, USA.

出版信息

Phys Rev E Stat Nonlin Soft Matter Phys. 2008 Jul;78(1 Pt 1):011908. doi: 10.1103/PhysRevE.78.011908. Epub 2008 Jul 16.

Abstract

We studied microrheological properties of F-actin across the isotropic-nematic phase transition region by video particle tracking (VPT) and by laser deflection particle tracking (LDPT). Both methods track the motion of thermally driven micron-sized beads, and convert the temporal mean square displacement (MSD) to shear moduli. The two methods give consistent results for the elastic modulus G' and less so for the loss modulus G'' . As the nematic order parameter increases with actin concentration, G'|| (measured parallel to the nematic director) and G' perpendicular (perpendicular to the director) grow apart, with G' perpendicular larger than G'||. The moduli scale with actin concentration as G'|| approximately c 0.54+/-0.13 and G' perpendicular approximately c 1.38+/-0.15. Furthermore, G' and G'' dependence on [Mg2+] were measured and compared for 1mg/ml isotropic and 4 mg/ml nematic F-actin solutions, respectively. In the isotropic phase, G' increases with [Mg2+] up to 6mM and then plateaus. In the nematic phase, G' perpendicular is larger than G'||, and both G' perpendicular and G'|| increase with [Mg2+] progressively up to 16 mM , above which F-actin form large bundles. In both isotropic and nematic phases, G'' only weakly depends on [Mg2+] . In conclusion, particle tracking microrheology reveals rich rheological features of F-actin affected by the isotropic-nematic phase transition and by tuning weak electrostatic interactions among the protein filaments.

摘要

我们通过视频粒子跟踪(VPT)和激光偏转粒子跟踪(LDPT)研究了F-肌动蛋白在各向同性-向列相转变区域的微观流变特性。两种方法都跟踪热驱动的微米级珠子的运动,并将时间均方位移(MSD)转换为剪切模量。对于弹性模量G',这两种方法给出的结果一致,而对于损耗模量G'',结果的一致性较差。随着向列序参数随肌动蛋白浓度增加,G'||(平行于向列指向矢测量)和G'垂直(垂直于指向矢)逐渐分开,G'垂直大于G'||。模量与肌动蛋白浓度的关系为G'||约为c^0.54±0.13,G'垂直约为c^1.38±0.15。此外,分别测量并比较了1mg/ml各向同性和4mg/ml向列相F-肌动蛋白溶液中G'和G''对[Mg2+]的依赖性。在各向同性相中,G'随[Mg2+]增加至6mM,然后趋于平稳。在向列相中,G'垂直大于G'||,且G'垂直和G'||均随[Mg2+]逐渐增加至16mM,超过该浓度F-肌动蛋白形成大束。在各向同性相和向列相中,G''仅微弱依赖于[Mg2+]。总之,粒子跟踪微观流变学揭示了受各向同性-向列相转变以及调节蛋白质细丝间弱静电相互作用影响的F-肌动蛋白丰富的流变学特征。

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