Center for Soft Condensed Matter Physics & Interdisciplinary Research, College of Physics, Optoelectronics and Energy, Soochow University, Suzhou, China.
Center for Soft Condensed Matter Physics & Interdisciplinary Research, College of Physics, Optoelectronics and Energy, Soochow University, Suzhou, China; National Laboratory of Solid State Microstructures and Department of Physics, Nanjing University, Nanjing, China.
J Mol Graph Model. 2018 Sep;84:145-151. doi: 10.1016/j.jmgm.2018.06.012. Epub 2018 Jun 14.
Understanding the interactions of dendrimers as drug/gene delivery vectors with proteins is important for functional optimization. Here, atomistic molecular dynamics simulations are employed to study the interactions between six positively-charged polyamidoamine dendrimers of the second generation (G2 PAMAM) and G-actin. We find that the structure of G-actin is relatively stable after dendrimers' binding. PAMAM dendrimers also do not significantly change the secondary structure of G-actin. Furthermore, we find the formation of dendrimer-actin complex is mainly driven by electrostatic interactions. Moreover, we suggest the secondary structure change of local domains of G-actin is probably responsible to the inhibition of actin polymerization.
了解树枝状聚合物作为药物/基因传递载体与蛋白质的相互作用对于功能优化很重要。在这里，采用原子分子动力学模拟研究了六种带正电荷的第二代聚酰胺胺树枝状聚合物（G2 PAMAM）与 G-肌动蛋白之间的相互作用。我们发现 G-肌动蛋白的结构在树枝状聚合物结合后相对稳定。PAMAM 树枝状聚合物也不会显著改变 G-肌动蛋白的二级结构。此外，我们发现树枝状聚合物-肌动蛋白复合物的形成主要是由静电相互作用驱动的。此外，我们认为 G-肌动蛋白局部结构域的二级结构变化可能是导致肌动蛋白聚合抑制的原因。
