Gu Zonglin, Perez-Aguilar Jose Manuel, Meng Lijun, Zhou Ruhong
Institute of Quantitative Biology, Department of Physics, and College of Life Sciences, Zhejiang University, Hangzhou 310027, China.
School of Chemical Sciences, Meritorious Autonomous University of Puebla (BUAP), University City, Puebla 72570, Mexico.
J Phys Chem B. 2020 Sep 3;124(35):7557-7563. doi: 10.1021/acs.jpcb.0c05850. Epub 2020 Aug 25.
Carbon nitride polyaniline (CN) nanosheets, since their recent successful synthesis, have been explored for biomedical applications. However, a thorough study of their interaction with biomolecules is still largely missing. Here, by using all-atom molecular dynamics simulations, we identified the mechanistic determinants of the interaction between a CN nanosheet and the prototypical protein villin headpiece (HP35). Our simulations revealed that, upon adsorption, the nanosheet can cause partial denaturation of HP35 by destructing its interior hydrogen bonds plus other native contacts and unwinding its helices. Our study also demonstrated that the CN/HP35 interaction energy showed stepwise changes during the binding process and held a strong correlation with the loss of HP35 native contacts. The findings shed light on the detailed molecular mechanism behind the interactions, which might benefit the future applications of CN-based nanostructures in biomedicine.
自从最近成功合成以来，氮化碳聚苯胺（CN）纳米片已被探索用于生物医学应用。然而，对其与生物分子相互作用的深入研究仍然非常缺乏。在这里，通过使用全原子分子动力学模拟，我们确定了CN纳米片与典型蛋白质绒毛蛋白头部结构域（HP35）之间相互作用的机制决定因素。我们的模拟表明，吸附后，纳米片可以通过破坏其内部氢键以及其他天然接触并解开其螺旋结构，导致HP35部分变性。我们的研究还表明，CN/HP35相互作用能在结合过程中呈现出逐步变化，并且与HP35天然接触的丧失密切相关。这些发现揭示了相互作用背后的详细分子机制，这可能有利于基于CN的纳米结构在生物医学中的未来应用。
