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Extraordinarily Stable Amyloid Fibrils Engineered from Structurally Defined β-Solenoid Proteins
Zeyu Peng1, Maria D R Peralta1, Michael D Toney1
1Department of Chemistry, University of California, Davis , 1 Shields Avenue, Davis, California 95616, United States.
Biochemistry
|October 25, 2017
Summary
Engineered protein fibrils from beta-solenoid proteins (BSPs) offer a stable and tunable alternative for nanomaterial fabrication. These novel protein nanostructures demonstrate remarkable resistance to heat, chemicals, and pH extremes, showing great potential for advanced applications.
Area of Science:
- Biomaterials Science
- Nanotechnology
- Protein Engineering
Background:
- Self-assembling biological molecules are promising for novel nanomaterial fabrication.
- Nucleic acid nanostructures face stability and functionalization challenges.
- Protein-based nanostructures offer chemical advantages but lag in design flexibility.
Purpose of the Study:
- To evaluate the stability and robustness of engineered beta-solenoid protein (BSP) fibrils.
- To explore the potential of BSPs for creating functional, stable nanomaterials.
- To compare the stability profiles of two distinct BSP fibril types.
Main Methods:
- Circular dichroism spectroscopy
- Transmission electron microscopy (TEM)
- Electrophoresis
Main Results:
- Both engineered BSP fibril types exhibited stability up to 90°C, with one type surviving autoclaving.
- Fibrils demonstrated stability against organic solvents, urea, and extreme pH conditions.
- One fibril type showed resistance to trypsin, while both were degraded by chymotrypsin and proteinase K.
Conclusions:
- Engineered BSPs are suitable candidates for bottom-up fabrication of robust nanomaterials.
- The defined sequence-structure relationship in BSPs allows for tunable properties.
- BSPs present a promising platform for developing functional, amyloid-based nanomaterials with enhanced stability.
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