Scheuer Karl, Helbing Christian, Firkowska-Boden Izabela, Jandt Klaus D
Chair of Materials Science, Otto Schott Institute of Materials Research, Friedrich Schiller University Jena Germany
Jena Center for Soft Matter, Friedrich Schiller University Jena Germany.
RSC Adv. 2021 Apr 16;11(23):14113-14120. doi: 10.1039/d0ra10749b. eCollection 2021 Apr 13.
Hybrid protein nanofibers (hPNFs) have been identified as promising nano building blocks for numerous applications in nanomedicine and tissue engineering. We have recently reported a nature-inspired, self-assembly route to create hPNFs from human plasma proteins, , albumin and hemoglobin. However, it is still unclear whether the same route can be applied to other plasma proteins and whether it is possible to control the composition of the resulting fibers. In this context, to further understand the hPNFs self-assembly mechanism and to optimize their properties, we report herein on ethanol-induced self-assembly of two different plasma proteins, , fibrinogen (FG) and fibronectin (FN). We show that by varying initial protein ratios, the composition and thus the properties of the resulting hPNFs can be fine-tuned. Specifically, atomic force microscopy, hydrodynamic diameter, and zeta potential data together revealed a strong correlation of the hPNFs dimensions and surface charge to their initial protein mixing ratio. The composition-independent prompt dissolution of hPNFs in ultrapure water, in contrast to their stability in PBS, indicates that the molecular arrangement of FN and FG in hPNFs is mainly based on electrostatic interactions. Supported by experimental data we introduce a feasible mechanism that explains the interactions between FN and FG and their self-assembly to hPNFs. These findings contribute to the understanding of dual protein interactions, which can be beneficial in designing innovative biomaterials with multifaceted biological and physical characteristics.
杂合蛋白质纳米纤维（hPNFs）已被视为在纳米医学和组织工程众多应用中颇具前景的纳米构建单元。我们最近报道了一种受自然启发的自组装途径，可从人血浆蛋白、白蛋白和血红蛋白制备hPNFs。然而，目前仍不清楚相同的途径是否可应用于其他血浆蛋白，以及是否有可能控制所得纤维的组成。在此背景下，为进一步了解hPNFs的自组装机制并优化其性能，我们在此报告乙醇诱导的两种不同血浆蛋白，即纤维蛋白原（FG）和纤连蛋白（FN）的自组装。我们表明，通过改变初始蛋白质比例，可以微调所得hPNFs的组成，进而调整其性能。具体而言，原子力显微镜、流体动力学直径和zeta电位数据共同揭示了hPNFs的尺寸和表面电荷与其初始蛋白质混合比例之间存在强相关性。与hPNFs在PBS中的稳定性相反，其在超纯水中与组成无关的快速溶解表明，hPNFs中FN和FG的分子排列主要基于静电相互作用。在实验数据的支持下，我们引入了一种可行的机制，解释了FN和FG之间的相互作用以及它们自组装形成hPNFs的过程。这些发现有助于理解双蛋白相互作用，这对于设计具有多方面生物学和物理特性的创新生物材料可能有益。
