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Updated: Jan 22, 2026
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Genotyping Single Nucleotide Polymorphisms in the Mitochondrial Genome by Pyrosequencing
Published on: February 10, 2023
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The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism
Mariana Pigozzi Cali1, Jim Monistrol1, Fabio Strati1
1CSSB Centre for Structural Systems Biology, Deutsches Elektronen-Synchrotron DESY, Hamburg, Germany.
Sub-Cellular Biochemistry
|January 20, 2026
Summary
Amyloids exhibit remarkable structural plasticity, forming diverse polymorphs with varied biological functions beyond disease. This adaptability highlights their ancient role in biological regulation and innovation.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Amyloids traditionally linked to neurodegenerative diseases.
- Amyloids also have crucial roles in microbial virulence, immunity, and cellular organization.
- Protein sequence can lead to multiple amyloid structures (polymorphs) with different functions.
Purpose of the Study:
- Explore structural and functional plasticity of amyloids.
- Elucidate polymorphic behavior in pathogenic and functional contexts.
- Examine structure-function relationships across evolution.
Main Methods:
- Cryo-electron microscopy (cryo-EM)
- Nuclear Magnetic Resonance (NMR)
- Microcrystallography
Main Results:
- High-resolution structures reveal amyloid polymorphism.
- Bacterial amyloids stabilize biofilms and modulate host-pathon interactions.
- Antimicrobial peptides form reversible fibrils with cytotoxic/immune functions.
- Amyloid-nucleic acid co-assemblies implicated in immune recognition and origin of life.
Conclusions:
- Amyloid polymorphism is a general mechanism for biological regulation.
- Understanding fibril states offers insights into health and disease.
- Amyloids are versatile scaffolds for adaptation and innovation, not just pathological end-products.
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