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Structural Flexibility and Disassembly Kinetics of Single Ferritin Molecules Using Optical Nanotweezers
Arman Yousefi1, Ze Zheng1, Saaman Zargarbashi1
1Advanced Optics and Photonics Laboratory, Department of Engineering, School of Science and Technology, Nottingham Trent University, Nottingham NG118NS, United Kingdom.
ACS Nano
|June 8, 2024
Summary
Researchers studied how chemicals affect ferritin, a protein shell that stores iron. They found ascorbic acid and low pH cause ferritin to change shape and break apart, revealing its disassembly process at the single-molecule level.
Area of Science:
- Biochemistry
- Structural Biology
- Nanotechnology
Background:
- Ferritin is a protein shell crucial for iron storage and release.
- Understanding chemical effects on ferritin structure is vital for iron-related disease research.
- Single-protein level analysis of ferritin dynamics and iron release is underexplored.
Purpose of the Study:
- To investigate the impact of ascorbic acid and pH on individual ferritin conformational dynamics.
- To elucidate the single-molecule disassembly pathway and kinetics of ferritin.
Main Methods:
- Utilized optical nanotweezers with double-nanohole (DNH) structures.
- Examined conformational dynamics of single ferritin molecules.
Main Results:
- Ferritin dynamics increased with rising ascorbic acid concentration.
- At pH 2.0, ferritin showed significant fluctuations and stepwise disassembly.
- Identified four key fragments during disassembly: 22-mer, 12-mer, tetramer, and dimer.
- Provided single-molecule evidence for cooperative ferritin disassembly.
Conclusions:
- Ascorbic acid and low pH induce significant structural changes and disassembly in ferritin.
- The study reveals the stepwise disassembly pathway and kinetics of single ferritin molecules.
- This research aids in understanding ferritin's role in iron metabolism and developing treatments for associated diseases.
