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, i.e., 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, i.e., 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.
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