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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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Amyloid Fibrils03:03

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Related Experiment Video

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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
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Published on: June 23, 2022

Changes in interfacial properties of alpha-synuclein preceding its aggregation.

Emil Palecek1, Veronika Ostatná, Michal Masarík

  • 1Institute of Biophysics, Academy of Sciences of the Czech Republic v.v.i., Kralovopolska 135, 612 65 Brno, Czech Republic. palecek@ibp.cz

The Analyst
|December 19, 2007
PubMed
Summary

Electrochemical methods detect early alpha-synuclein (AS) changes during Parkinson's disease (PD) pathogenesis. These techniques offer a sensitive way to study AS aggregation and identify pathogenic oligomers.

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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
15:04

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

Area of Science:

  • Biochemistry
  • Neuroscience
  • Electrochemistry

Background:

  • Parkinson's disease (PD) involves alpha-synuclein (AS) amyloid fibril formation.
  • Oligomeric AS intermediates, not fibrils, are suspected PD pathogens.
  • Efficient detection methods for pathogenic AS oligomers are currently lacking.

Purpose of the Study:

  • To investigate the interfacial properties of wild-type AS during aggregation.
  • To explore the utility of electrochemical analysis for detecting AS aggregation intermediates.
  • To correlate electrochemical changes with AS oligomerization and fibril formation.

Main Methods:

  • Electrochemical analysis of AS tyrosine residue oxidation at carbon electrodes.
  • Measurement of AS adsorption and electrocatalytic hydrogen evolution at hanging mercury drop electrodes (HMDEs).
  • Dynamic light scattering (DLS) to monitor AS oligomerization.

Main Results:

  • Electrochemical signals (tyrosine oxidation, AS adsorption, electrocatalysis) decreased during AS incubation.
  • HMDEs showed high sensitivity to pre-aggregation AS changes, with early shifts in electrocatalytic peak H.
  • Observed electrochemical changes correlated with AS oligomerization detected by DLS.

Conclusions:

  • Early electrochemical changes reflect AS protein destabilization and disruption of interactions.
  • Subsequent electrochemical shifts are linked to the onset of AS oligomerization.
  • Electrochemical methods provide a novel, simple, and sensitive tool for studying amyloid formation in PD.