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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.

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|October 25, 2017
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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.

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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.