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Related Concept Videos

Amyloid Fibrils03:03

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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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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Membrane lipid co-aggregation with α-synuclein fibrils.

Erik Hellstrand1, Agnieszka Nowacka, Daniel Topgaard

  • 1Division of Biophysical Chemistry, Center of Chemistry and Chemical Engineering, Lund University, Lund, Sweden.

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|October 23, 2013
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Summary

This study reveals that amyloid formation with lipids is a co-aggregation process, not just protein adsorption. This finding impacts understanding of amyloid diseases and lipid-protein interactions.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Materials Science

Background:

  • Amyloid deposits in human diseases often contain membrane lipids.
  • Lipid-protein co-aggregation influences the structure and function of both membranes and amyloid deposits.
  • The mechanisms and molecular structures of lipid-amyloid co-aggregation remain poorly understood.

Purpose of the Study:

  • To investigate the in vitro co-aggregation mechanism between phospholipid model membranes and alpha-synuclein.
  • To elucidate the molecular structure and dynamics of lipid-protein co-aggregates.

Main Methods:

  • Incubation of monomeric alpha-synuclein with anionic phospholipid model membranes.
  • Phospholipid quantification.
  • Solid-state NMR with polarization transfer.
  • Cryo-transmission electron microscopy (cryo-TEM).

Main Results:

  • Spontaneous uptake of phospholipids into alpha-synuclein amyloid fibrils.
  • Evidence of saturable co-aggregation dependent on lipid composition.
  • At low lipid-protein ratios, phospholipids closely associate with fibrils, reducing mobility and altering morphology.
  • At higher ratios, vesicles adsorb to fibrils.

Conclusions:

  • Amyloid formation in the presence of lipids is a co-aggregation process.
  • Lipid-protein co-aggregates exhibit unique structures, dynamics, and morphologies compared to individual components.
  • Findings offer new perspectives on amyloid pathology and lipid-protein interactions.