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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...
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...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview

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Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
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Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

In Vitro-Prepared A30P Alpha-Synuclein Fibrils Adopt the Conserved and Disease-Relevant Greek Key Fold.

Moses H Milchberg1,2, Owen A Warmuth1,2, Collin G Borcik1

  • 1Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.

The Journal of Physical Chemistry. B
|July 2, 2026
PubMed
Summary

Parkinson disease (PD) is linked to alpha-synuclein (Asyn) protein fibrils. Researchers determined the high-resolution structure of the A30P mutant Asyn fibril, revealing a conserved Greek key fold similar to other PD-associated structures.

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Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

Area of Science:

  • Neuroscience
  • Structural Biology
  • Biochemistry

Background:

  • Parkinson disease (PD) is characterized by alpha-synuclein (Asyn) protein aggregation into fibrils.
  • Previous studies determined Asyn fibril structures using SSNMR and cryo-EM, aiding drug development and understanding disease specificity.
  • Structural polymorphism of Asyn fibrils is a key feature in PD pathogenesis.

Purpose of the Study:

  • To determine the high-resolution solid-state nuclear magnetic resonance (SSNMR) structure of the A30P hereditary mutant Asyn fibril.
  • To develop a method for rapid comparison of SSNMR spectra between different Asyn polymorphs.
  • To investigate the structural similarity of the A30P mutant fibril to other Asyn fibril structures.

Main Methods:

  • High-resolution SSNMR spectroscopy was employed to determine the fibril structure.
  • 3D 13C-13C-13C correlation experiments were used to derive distance restraints.
  • A comprehensive method for rapid SSNMR spectral comparison was developed and validated.

Main Results:

  • The A30P mutant Asyn fibril adopts a Greek key topology.
  • The P30 mutation site was not found within the fibril core.
  • The A30P fibril structure is highly similar to other experimentally determined Asyn fibril structures, including those with different hereditary mutations.

Conclusions:

  • The determined A30P Asyn fibril structure provides insights into early-onset PD.
  • A conserved accessible fold exists across various Asyn fibril polymorphs, suggesting common structural features relevant to PD.
  • The findings support a conserved structural basis for Asyn fibril formation in Parkinson disease.