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Extremophilic behavior of catalytic amyloids sustained by backbone structuring.

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Catalytic amyloids exhibit remarkable stability and activity at extreme temperatures and in organic solvents, outperforming traditional enzymes. Their unique structure, stabilized by reorganized backbone hydrogen bonds, enables enzyme-like functions in harsh conditions for synthetic applications.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Biophysics

Background:

  • Enzyme function depends on precise chemical arrangements stabilized by protein backbone hydrogen bonds.
  • Amyloids, known for self-associative hydrogen bonds, can mimic enzyme activity and stability.
  • Previous studies showed some stability, but extreme properties and molecular basis remained unclear.

Purpose of the Study:

  • To define the extremophilic properties of catalytic amyloids.
  • To elucidate the molecular mechanisms behind their extreme activity and stability.
  • To explore their potential for synthetic applications.

Main Methods:

  • Investigated catalytic amyloid activity across a range of temperatures and solvents.
  • Utilized in situ non-linear 2D infrared spectroscopy (2DIR) to analyze backbone vibrational states.
  • Employed molecular modeling to understand structural changes and bonding dynamics.

Main Results:

  • Catalytic amyloid activity persists and optimizes at high temperatures (81 °C), showing 30-fold increase.
  • Amyloids retain structure and activity above 100 °C and in co-solvents.
  • 2DIR revealed reorganized backbone hydrogen bonds and an emergent vibrational mode at 1612 cm⁻¹.
  • Molecular modeling confirmed stabilization through restructured hydrogen bonds in organic solvents.

Conclusions:

  • Catalytic amyloids possess extreme stability and activity, surpassing thermophilic enzymes.
  • Restructuring of backbone hydrogen bonds is key to maintaining function in harsh environments.
  • These properties make amyloids promising for synthetic applications requiring robust biocatalysts.