The known antiviral vaccines based on ferritin-fused antigens are synthesized in the HEK (Human Embryonic Kidney cells) expression system, making them difficult for large-scale production. In this work, we present the potential vaccine based on Escherichia coli ferritin fused with a receptor-binding domain (RBD) of the spike glycoprotein from SARS-CoV-2 expressed and purified from E. coli cells. This chimeric protein is a potential perspective candidate for creating a platform for rapid development of vaccines against coronaviruses and other pathogens. Expression and purification from E. coli cells together with small-angle X-ray scattering experiments showed multimeric assemblies of these chimeric proteins. Additionally to characterize the nanoparticle we used computer molecular modeling, molecular dynamics simulations and quantum biochemical analysis which provide new information about the interaction driving the complex formation and stabilization as well as the type of interactions that support it. Besides, computational analysis may help in understanding of the best conformations and domains involved in the interactions which may help to engineer the enhanced complex.