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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Related Experiment Video

Updated: Jun 28, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Published on: September 12, 2019

alpha-Synuclein misfolding: single molecule AFM force spectroscopy study.

Junping Yu1, Sarka Malkova, Yuri L Lyubchenko

  • 1Department of Pharmaceutical Sciences, University of Nebraska Medical Center, Omaha, NE 68198, USA.

Journal of Molecular Biology
|October 25, 2008
PubMed
Summary
This summary is machine-generated.

Protein misfolding, a key step in Parkinson's disease, was studied using single-molecule force spectroscopy. Alpha-synuclein dimers showed increased stability and lifetimes, suggesting they act as nuclei for aggregation.

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Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One &#945;-Synuclein Monomer at a Time
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Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

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Last Updated: Jun 28, 2026

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Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One &#945;-Synuclein Monomer at a Time
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Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

Area of Science:

  • Biophysics
  • Neuroscience
  • Biochemistry

Background:

  • Protein misfolding and aggregation are implicated in neurodegenerative diseases like Parkinson's.
  • Alpha-synuclein misfolding is central to Parkinson's pathogenesis.
  • Understanding misfolded protein dynamics is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To investigate the misfolding mechanism of alpha-synuclein.
  • To detect misfolded alpha-synuclein states using single-molecule force spectroscopy.
  • To characterize the stability and aggregation pathways of alpha-synuclein.

Main Methods:

  • Single-molecule force spectroscopy (SMFS) was employed.
  • Alpha-synuclein molecules were immobilized at their C-termini.
  • Atomic force microscopy (AFM) was used to probe interprotein interactions and measure dimer lifetimes.

Main Results:

  • Enhanced interprotein interactions detected misfolded alpha-synuclein states.
  • Misfolded alpha-synuclein dimers exhibited lifetimes in the range of seconds.
  • Dimer lifetimes were significantly longer than those of monomeric alpha-synuclein.
  • Two distinct dimer lifetimes suggest diverse aggregation pathways.

Conclusions:

  • Misfolded alpha-synuclein dimers are more stable than monomeric forms.
  • These stable dimers can act as nuclei for alpha-synuclein aggregation.
  • Alpha-synuclein aggregation may proceed via multiple pathways, leading to varied aggregate structures.