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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: May 18, 2026

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
04:41

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

Preparing synthetic Aβ in different aggregation states.

W Blaine Stine1, Lisa Jungbauer, Chunjiang Yu

  • 1Department of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, IL, USA.

Methods in Molecular Biology (Clifton, N.J.)
|October 23, 2010
PubMed
Summary
This summary is machine-generated.

Researchers developed protocols for creating uniform amyloid-beta peptide (Aβ) assemblies, crucial for Alzheimer's disease (AD) research. These methods yield specific oligomeric and fibrillar Aβ42 structures for functional studies.

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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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Last Updated: May 18, 2026

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
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Published on: July 14, 2010

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Biology

Background:

  • Alzheimer's disease (AD) research heavily relies on understanding amyloid-beta peptide (Aβ) structure.
  • The 42 amino acid Aβ (Aβ42) is genetically and pathologically linked to AD.
  • Aβ42 function is dependent on its structural assembly state.

Purpose of the Study:

  • To outline reproducible protocols for generating homogenous preparations of oligomeric and fibrillar Aβ42.
  • To enable consistent production of specific Aβ42 structural assemblies for biochemical, cellular, and in vivo studies.
  • To develop tools for connecting Aβ42 structure to function.

Main Methods:

  • Monomerization of purified Aβ42 using a strong solvent to erase structural history.
  • Optimization of solution conditions to produce homogenous oligomeric and fibrillar Aβ42 assemblies.
  • Characterization using atomic force microscopy (AFM) to identify discrete species.
  • Development of a protocol for fluorescently labeling Aβ42 without altering structure or function.

Main Results:

  • Consistent production of homogenous oligomeric and fibrillar Aβ42 assemblies.
  • Demonstration of functional differences between oligomeric and fibrillar Aβ42.
  • Validated fluorescently labeled Aβ42 reagents that maintain structural integrity and function.

Conclusions:

  • The developed protocols provide critical tools for Alzheimer's disease research.
  • Homogenous Aβ42 preparations allow for precise structure-function relationship studies.
  • Fluorescently labeled Aβ42 facilitates detailed investigation of Aβ42 interactions and mechanisms.