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Related Experiment Video

Updated: Aug 24, 2025

Ferritinophagy: Assessing the Selective Degradation of Iron by Autophagy in Human Fibroblasts

Ferritinophagy: Assessing the Selective Degradation of Iron by Autophagy in Human Fibroblasts

Published on: February 23, 2024

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

Vsevolod V Sudarev¹, Sofya M Dolotova², Siarhei M Bukhalovich¹

¹Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, 141700 Dolgoprudny, Russia.

International Journal of Biological Macromolecules

|October 24, 2022

Summary

Ferritin, an iron-storing protein, is vital in health and disease. Understanding its self-assembly mechanisms is key for biotechnological and pharmaceutical applications, offering potential control over its function.

Keywords:

Biotechnology Ferritin Self-assembly

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Area of Science:

Biochemistry
Molecular Biology
Biotechnology

Background:

Ferritin is a crucial protein complex for iron storage in organisms.
It impacts metabolic pathways, inflammation, stress, and diseases like cancer and neurodegeneration.
Ferritin's structure and function are central to cellular iron homeostasis.

Purpose of the Study:

To review the multifaceted roles of ferritin in diseases and cellular iron regulation.
To explore the structural features and biotechnological applications of ferritin.
To analyze ferritin self-assembly mechanisms and their control for pharmaceutical applications.

Main Methods:

Literature review of ferritin's role in disease and cellular iron regulation.
Analysis of ferritin's structural characteristics and self-assembly pathways.
Comparison of proposed ferritin self-assembly kinetics and intermediate states.

Main Results:

Ferritin's involvement in critical biological processes and disease pathogenesis is highlighted.
Molecular mechanisms of ferritin self-assembly are identified as crucial for biotechnological and pharmaceutical uses.
The dependence of assembly pathways on monomer interface context and intermediate oligomer stability is discussed.

Conclusions:

Understanding ferritin self-assembly is essential for developing novel biotechnological and pharmaceutical strategies.
Control over ferritin self-assembly, potentially via intermediate states, offers promising avenues for applications.
Ferritin's role extends from fundamental biology to advanced therapeutic and diagnostic development.