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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. 
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Protein Folding01:22

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Protein Folding01:25

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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.
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Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
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Related Experiment Video

Updated: Nov 15, 2025

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-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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Structural insights into α-synuclein monomer-fibril interactions.

Pratibha Kumari1, Dhiman Ghosh1, Agathe Vanas1

  • 1Department of Chemistry and Applied Biosciences, Laboratory of Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland.

Proceedings of the National Academy of Sciences of the United States of America
|March 2, 2021
PubMed
Summary

Parkinson's disease involves protein aggregation. This study shows alpha-synuclein monomers unfold and align on fibrils, accelerating aggregation through secondary nucleation.

Keywords:
Parkinson’s diseaseprotein aggregationsecondary nucleationα-synuclein

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Protein aggregation into amyloid fibrils is linked to neurodegenerative diseases like Parkinson's disease.
  • Secondary nucleation significantly accelerates protein aggregation by monomer absorption onto existing fibrils.

Purpose of the Study:

  • To investigate the interaction between monomeric alpha-synuclein and its fibrillar form using advanced spectroscopy.
  • To elucidate the role of these interactions in the secondary nucleation pathway of alpha-synuclein aggregation.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Electron Paramagnetic Resonance (EPR) spectroscopy.

Main Results:

  • Monomeric alpha-synuclein (α-Syn) interacts transiently with amyloid fibrils.
  • Interactions occur between the positively charged N-terminus of α-Syn monomers and the negatively charged C-termini of fibrils.
  • These interactions promote monomer unfolding and alignment on the fibril surface, increasing local concentration.

Conclusions:

  • Intramolecular unfolding of alpha-synuclein is a critical factor in secondary nucleation.
  • Understanding these interactions provides insights into Parkinson's disease pathogenesis.
  • The findings highlight a mechanism accelerating amyloid fibril formation.