Center for Soft Condensed Matter Physics and Interdisciplinary Research, School of Physical Science and Technology, Soochow University, Suzhou 215006, China.
National Laboratory of Solid State Microstructures and Department of Physics, Collaborative Innovation Center of Advanced Microstructures, Nanjing University, Nanjing 210093, China.
Langmuir. 2024 Jul 23;40(29):15205-15213. doi: 10.1021/acs.langmuir.4c01642. Epub 2024 Jul 11.
The size or the curvature of nanoparticles (NPs) plays an important role in regulating the composition of the protein corona. However, the molecular mechanisms of how curvature affects the interaction of NPs with serum proteins still remain elusive. In this study, we employ all-atom molecular dynamics simulations to investigate the interactions between two typical serum proteins and PEGylated Au NPs with three different surface curvatures (0, 0.1, and 0.5 nm, respectively). The results show that for proteins with a regular shape, the binding strength between the serum protein and Au NPs decreases with increasing curvature. For irregularly shaped proteins with noticeable grooves, the binding strength between the protein and Au NPs does not change obviously with increasing curvature in the cases of smaller curvature. However, as the curvature continues to increase, Au NPs may act as ligands firmly adsorbed in the protein grooves, significantly enhancing the binding strength. Overall, our findings suggest that the impact of NP curvature on protein adsorption may be nonmonotonic, which may provide useful guidelines for better design of functionalized NPs in biomedical applications.
纳米颗粒（NPs）的大小或曲率在调节蛋白质冠的组成方面起着重要作用。然而，曲率如何影响 NPs 与血清蛋白相互作用的分子机制仍不清楚。在这项研究中，我们采用全原子分子动力学模拟来研究两种典型的血清蛋白与具有三种不同表面曲率（分别为 0、0.1 和 0.5nm）的聚乙二醇化 Au NPs 之间的相互作用。结果表明，对于形状规则的蛋白质，血清蛋白与 Au NPs 之间的结合强度随曲率的增加而降低。对于具有明显凹槽的形状不规则的蛋白质，在较小曲率的情况下，曲率的增加对蛋白质与 Au NPs 之间的结合强度没有明显影响。然而，随着曲率的继续增加，Au NPs 可能作为配体牢固地吸附在蛋白质凹槽中，显著增强结合强度。总体而言，我们的研究结果表明，NP 曲率对蛋白质吸附的影响可能是非单调的，这可能为更好地设计生物医学应用中的功能化 NPs 提供有用的指导。
