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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 and Protein Structure02:15

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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Related Experiment Video

Updated: Oct 12, 2025

Analysis of &#946;-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

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Amyloid β 42 fibril structure based on small-angle scattering.

Veronica Lattanzi1,2, Ingemar André3, Urs Gasser4

  • 1Biochemistry and Structural Biology, Lund University, SE-22100 Lund, Sweden; veronica.lattanzi@biochemistry.lu.se.

Proceedings of the National Academy of Sciences of the United States of America
|November 24, 2021
PubMed
Summary

Researchers studied amyloid-beta 42 (Aβ42) fibrils, linked to Alzheimer's disease. Using small-angle scattering, they determined the fibril structure, revealing a stable two-filament arrangement crucial for understanding neurotoxicity and developing therapies.

Keywords:
SAXS/SANSamyloid-betaatomistic modelfibril structure in solutionnumber of filaments

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Area of Science:

  • Biophysics
  • Neuroscience
  • Structural Biology

Background:

  • Amyloid fibrils, particularly amyloid-beta 42 (Aβ42), are implicated in Alzheimer's disease pathogenesis.
  • Aβ42 fibril surface toxicity arises from the generation of toxic oligomers, highlighting the need for structural insights.
  • Understanding fibril structure is critical for developing targeted therapeutic strategies.

Purpose of the Study:

  • To determine the cross-section dimension and shape of Aβ42 fibrils.
  • To develop a detailed atomistic model of Aβ42 fibril structure.
  • To investigate the stability and arrangement of filaments within Aβ42 fibrils.

Main Methods:

  • Small-angle scattering (SAS) was employed to analyze Aβ42 fibrils prepared under specific conditions.
  • Continuum and atomistic modeling, including Rosetta optimization and fitting to SAS data, were used to elucidate fibril structure.
  • Solid-state NMR data (PDB ID 5kk3) served as a starting point for atomistic model development.

Main Results:

  • SAS data revealed an elliptical cross-section for Aβ42 fibrils with a mass-per-unit length consistent with two filaments, each containing two monomers arranged in planes.
  • Atomistic modeling resulted in a two-filament model with twofold rotation symmetry around the fibril axis, incorporating residues 11-42.
  • No observed polydispersity in filament number across samples suggests a stable, energetically favorable two-filament arrangement.

Conclusions:

  • The study provides a high-resolution atomistic model of Aβ42 fibrils, revealing a stable two-filament structure.
  • This structural characterization offers valuable insights into the mechanism of Aβ42 fibril toxicity.
  • The findings support the two-filament arrangement as a potential therapeutic target for Alzheimer's disease.