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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...

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Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Lipid-induced beta-amyloid peptide assemblage fragmentation.

Martin J O Widenbrant1, Jayakumar Rajadas, Christopher Sutardja

  • 1Department of Chemical Engineering, Stanford University, Stanford, CA, USA.

Biophysical Journal
|November 14, 2006
PubMed
Summary

Alzheimer's disease involves beta-amyloid peptides (Abeta) interacting with cell membranes. This study reveals Abeta aggregates immobilize fluid lipid membranes, offering new insights into disease mechanisms.

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Last Updated: Jul 18, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Alzheimer's disease, a leading cause of dementia, is linked to beta-amyloid peptide (Abeta) accumulation and cell membrane interactions.
  • Abeta peptides, derived from amyloid precursor proteins, undergo conformational changes leading to membrane binding and cellular degeneration.
  • The precise mechanisms by which Abeta aggregates disrupt membrane integrity remain unclear, despite membrane fluidity's known role in cellular pathophysiology.

Purpose of the Study:

  • To investigate the structural details of Abeta aggregate-lipid interactions.
  • To understand how Abeta aggregates affect membrane fluidity and integrity.

Main Methods:

  • Utilized atomic force microscopy (AFM) to observe Abeta aggregate-lipid interactions.
  • Employed transmission electron microscopy (TEM) to analyze structural changes.

Main Results:

  • Observed that fluid lipid monolayers develop immobile domains upon interaction with Abeta aggregates.
  • Found that Abeta fibrils fragment into smaller nano-assemblages when interacting with membrane lipids.

Conclusions:

  • Abeta aggregates significantly alter membrane structure by inducing immobility and fragmentation.
  • These findings suggest a reappraisal of Abeta aggregate-lipid interactions in Alzheimer's disease pathogenesis is warranted.