Objectives: The aim is to produce two chimeric EGF receptor growth factor molecules to test their effect on cell signaling, in order to create biologically active homogeneous and heterogeneous recombinant molecules of dimeric growth factors that could potentially inhibit receptor activity. In this study, we focused on examining the effect of homogeneous dimeric growth factors, in the form of fusion proteins, on the phosphorylation of the EGF receptor and the downstream RAS/MAPK signaling pathway in the CHO cell line. Results: The transfected cells of the CHO cell line were stimulated with the produced chimeric molecules containing flexible or rigid linker, followed by immunoblot analysis of the phosphorylation of the EGF receptor and the downstream RAS/MAPK signaling pathway. Materials and methods: A statistically significant result was observed in the difference of phosphorylation signal of the receptor and ERK kinase stimulated by EGF, in relation to chimeric molecules 1 and 2. Stimulation of EGF receptors by chimeras 1 and 2, in contrast to stimulation by monomeric growth factor, did not result in activation of EGF receptors. The hypothesis that there is a possibility of inhibition of receptor activation by a chimeric molecule with rigid linker was confirmed; furthermore it was determined that a chimeric molecule with a flexible linker has the same effect. Despite the fact that receptor stimulation with chimeric molecules did not induce receptor phosphorylation, the results showed activation of the downstream RAS/MAPK signaling pathway after 5 minutes. It is possible that chimeric molecules 1 and 2 interact with the receptor on the membrane and cause the activation of the RAS/MAPK signaling pathway by an unknown mechanism. In addition, the absence of ERK kinase phosphorylation at later time intervals could be interpreted by the absence of receptor endocytosis due to the biophysical properties of the linker structure. The results of the activation of mutated forms of the EGF receptor showed that recombinant homodimeric molecules 1 and 2 do not affect the three-dimensional structure of the receptor. Conclusions: Homodimeric recombinant molecules 1 and 2 do not have the ability to activate the EGF receptor and induce downstream signaling pathways of the cell. Furthermore, they do not cause alterations in the three-dimensional structure of the receptor. If the binding of these molecules to the population of EGF receptors on the membrane, and the absence of activation of other downstream signaling pathways is ultimately confirmed, the results of this study could lay the foundations for the development of a completely new model of inhibition of EGF receptor activation, esentially a new form of tumor treatment.