Self-assembly of toroidal proteins explored using native mass spectrometry

Area of Science:

• Biochemistry
• Nanotechnology
• Structural Biology

Background:

• Peroxiredoxins are well-characterized toroidal proteins capable of self-assembly into diverse quaternary structures.
• These protein assemblies, including nanotubes, are of significant interest as building blocks for nanotechnology.
• Current tools for characterizing these complex protein assemblies are limited.

Purpose of the Study:

• To investigate the self-assembly of peroxiredoxin proteins using advanced analytical techniques.
• To characterize the structural properties and assembly dynamics of peroxiredoxin nanotubes.
• To explore the potential of peroxiredoxins as tunable building blocks for nanotechnology applications.

Main Methods:

• Native mass spectrometry was employed to analyze peroxiredoxin assemblies.
• Complementary solution techniques were utilized for comprehensive characterization.
• Collision-induced dissociation experiments were performed on peroxiredoxin rings.

Main Results:

• Tube formation by peroxiredoxin proteins was demonstrated to be fully reversible.
• Assembly of peroxiredoxin toroids was found to be tunable by pH and the presence of a histidine tag.
• Peroxiredoxin rings exhibited an unusual symmetrical disassembly pathway, suggesting a hexamer of dimers structure.

Conclusions:

• This study provides a foundation for the rational design of peroxiredoxin-based nanostructures.
• The reversible and tunable nature of peroxiredoxin self-assembly is highlighted for molecular switch applications.
• Precise characterization of peroxiredoxin structures is essential for harnessing their self-assembly in nanotechnology.