Abstract <p>Ferritin is an iron-storage protein complex performing vital functions in various living organisms. Its properties are significantly defined by a topology of the protein globule and the structural arrangement of subunits on its surface. Understanding the mechanisms of ferritin self-assembly could open up new ways of functionalization of its surface coating with a number of applications in biotechnology. In this study, we investigated the self-assembly of ferritin using the Smoluchowski coagulation model. We numerically solved the Smoluchowski differential equations for various models, involving the formation of hybrid ferritins with two types of subunits (for instance, H and L). Our model incorporates different reaction schemes and provides insights into the kinetics of oligomer assembly. The results reveal that our model can accurately describe the temporal dynamics of ferritin assembly, predicting the formation of intermediate states and fully assembled globules. The extension of the model using a four-dimensional coagulation kernel enables a detailed description of hybrid ferritin assembly, offering a new perspective on the complexity of self-assembly processes in heterooligomeric protein systems. Overall, our findings provide a robust framework for understanding the dynamics of ferritin assembly, offering insights that could be generalized to other carriers and help in designing more effective experimental approaches to study these mechanisms.</p>