Ferritin self-assembly, structure, function, and biotechnological applications

Ferritin is a vital protein complex responsible for storing iron in almost all living organisms. It plays a crucial role in various metabolic pathways, inflammation processes, stress response, and pathogenesis of cancer and neurodegenerative diseases. In this review we discuss the role of ferritin in diseases, cellular iron regulation, its structural features, and its role in biotechnology. We also show that molecular mechanisms of ferritin self -assembly are key for a number of biotechnological and pharmaceutical applications. The assembly pathways strongly depend on the interface context of ferritin monomers and the stability of its different intermediate oligomers. To date, several schemes of self-assembly kinetics have been proposed. Here, we compare different self-assembly mechanisms and discuss the possibility of self-assembly control by switching between deadlock intermediate states.

Automated summary

Ferritin is a crucial protein complex that stores iron and plays various roles in metabolic pathways, inflammation, stress response, and disease development. This review emphasizes the importance of ferritin in disease, cellular iron regulation, its structure, and its applications in biotechnology. The molecular mechanisms of ferritin self-assembly are essential for biotechnological and pharmaceutical purposes, and different self-assembly pathways have been proposed. This review compares these mechanisms and discusses the potential to control self-assembly by switching between intermediate states.