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Related Concept Videos

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Modulating amyloids' formation path with sound energy.

Anna Kozell1, Dror Eliaz1, Aleksei Solomonov1

  • 1Department of Molecular Chemistry and Materials Science, Faculty of Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel.

Proceedings of the National Academy of Sciences of the United States of America
|January 11, 2023
PubMed
Summary
This summary is machine-generated.

Ultrasound unexpectedly disrupts amyloid structures, transforming harmful β-sheet aggregates into non-amyloidogenic protein folds. This controlled structural change offers new therapeutic possibilities for amyloid diseases.

Keywords:
amyloidbeta-sheet conformationcavitationfibrillar protein self-assemblyultrasound

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Protein misfolding and aggregation into amyloid fibrils are implicated in diseases like amyloidosis.
  • The precise conditions driving amyloid formation and the self-assembly pathway remain unclear.
  • Ultrasound is typically used to destabilize protein structures and promote amyloid growth.

Purpose of the Study:

  • To investigate the unexpected effects of ultrasound on lysozyme amyloid species at various aggregation stages.
  • To understand the mechanisms by which ultrasound influences protein structure and amyloid formation.
  • To establish conditions for controlling ultrasound-induced structural modifications in amyloid proteins.

Main Methods:

  • Infrared and X-ray analyses to assess chemical, mechanical, and thermal effects of ultrasound on lysozyme.
  • Solution X-ray scattering to determine the structure, mass fraction, and morphology of lysozyme assemblies.
  • Nanomechanical analysis to correlate β-sheet content with the elastic modulus of protein assemblies.

Main Results:

  • Ultrasound induced irreversible disruption of β-sheet folds in fibrillar lysozyme, converting them into non-amyloidogenic monomers.
  • Observed changes in protein self-assembly kinetics, including prolonged nucleation and accelerated fibril growth.
  • Established a correlation between β-sheet content and the elastic modulus of ultrasound-modified protein assemblies.

Conclusions:

  • Ultrasound can induce non-amyloidogenic structural transformations in amyloid proteins, contrary to its typical role in promoting aggregation.
  • Controlling specific ultrasound effects allows for targeted structural modifications of amyloid β-sheet-rich proteins.
  • This research provides a foundation for utilizing ultrasound to therapeutically alter protein structures in amyloidosis.