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High pressure promotes circularly shaped insulin amyloid
Ralf Jansen1, Stefan Grudzielanek, Wojciech Dzwolak
1Physical Chemistry I, Department of Chemistry, University of Dortmund, Otto-Hahn-Str. 6, D-44227 Dortmund, Germany.
Journal of Molecular Biology
|April 7, 2004
Summary
High hydrostatic pressure transforms insulin into circular amyloids, distinct from typical linear protein aggregates. This finding impacts our understanding of protein structures and high-pressure food processing.
Area of Science:
- Biophysics
- Structural Biology
- Materials Science
Background:
- Amyloids are beta-sheet-rich protein aggregates with a common linear fibrillar morphology.
- Amyloids are implicated in degenerative diseases and prion-based inheritance.
Purpose of the Study:
- To investigate the effect of high hydrostatic pressure on insulin amyloid formation.
- To characterize the morphology of pressure-induced insulin amyloids.
Main Methods:
- High hydrostatic pressure was applied to insulin.
- The morphology of the resulting amyloid structures was analyzed.
Main Results:
- High hydrostatic pressure induced the formation of insulin amyloids with a unique circular morphology.
- Ring-shaped structures with radii of 340-420 nm were most abundant.
- Bent fibrils (20-100 nm) were also observed alongside the circular amyloids.
Conclusions:
- Pressure can significantly alter amyloid morphology, suggesting anisotropic void volumes in regular amyloid fibers.
- This pressure-induced conformational change may influence amyloid templating and infectivity.
- The findings raise questions about the implications for high-pressure food processing.