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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Stable, metastable, and kinetically trapped amyloid aggregate phases.

Tatiana Miti1, Mentor Mulaj, Jeremy D Schmit

  • 1Department of Physics, University of South Florida , Tampa, Florida 33620, United States.

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Protein self-assembly into amyloid fibrils is linked to diseases. This study reveals distinct phases for amyloid oligomers and fibrils, controlled by concentration and salt, offering insights into disease mechanisms.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Protein self-assembly into amyloid fibrils is implicated in various human diseases, including Alzheimer's and type II diabetes.
  • Early-stage compact oligomeric species are considered the primary toxic entities in amyloid formation.
  • The relationship between transient oligomers and stable amyloid fibrils remains poorly understood.

Purpose of the Study:

  • To elucidate the relationship between amyloid oligomers and fibrils.
  • To define the phase boundaries for amyloid oligomer and fibril formation.
  • To investigate the factors influencing the transition from oligomeric to fibrillar states.

Main Methods:

  • Experimental determination of phase boundaries for lysozyme amyloid oligomers and fibrils.
  • Analysis of salt and protein concentration effects on aggregation.
  • Comparison with colloidal models incorporating charge repulsion and metastability.

Main Results:

  • Amyloid oligomers and fibrils occupy distinct regions in a phase diagram.
  • Formation of lysozyme amyloid oligomers and fibrils is dependent on crossing specific salt and protein concentration thresholds.
  • Oligomeric aggregates are metastable and structurally distinct from rigid fibrils.

Conclusions:

  • Amyloid self-assembly exhibits phase behavior analogous to colloidal systems.
  • Salt concentration and protein concentration critically control the formation and stability of different amyloid species.
  • Understanding these phase boundaries is crucial for deciphering the molecular mechanisms of amyloid-related diseases.