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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...
Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...
Mutations01:39

Mutations

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Related Experiment Video

Updated: May 20, 2026

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

Published on: July 14, 2010

Point mutations in Aβ induce polymorphic aggregates at liquid/solid interfaces.

Elizabeth A Yates1, Elena M Cucco, Justin Legleiter

  • 1The C. Eugene Bennett Department of Chemistry, West Virginia University, 217 Clark Hall, P.O. Box 6045, Morgantown, West Virginia 26506, United States.

ACS Chemical Neuroscience
|July 11, 2012
PubMed
Summary
This summary is machine-generated.

Alzheimer's disease (AD) mutations alter amyloid-beta (Aβ) aggregation rates in solution but not morphology. However, on anionic surfaces, these mutations significantly change Aβ aggregate structures, highlighting the role of surfaces in AD pathology.

Keywords:
Alzheimer’s diseaseAtomic force microscopypoint mutations in Aβpolymorphic aggregate formationprotein aggregationβ-amyloid

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Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain
09:35

Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain

Published on: October 24, 2017

Area of Science:

  • Neuroscience
  • Biochemistry
  • Materials Science

Background:

  • Alzheimer's disease (AD) is characterized by amyloid plaques, primarily composed of β-amyloid (Aβ) peptide aggregates.
  • Aβ aggregation into various polymorphic structures is influenced by environmental factors, notably surfaces.
  • Specific mutations in Aβ, such as Arctic (E22G) and Italian (E22K), are linked to hereditary forms of AD and cerebral amyloid angiopathy (CAA).

Purpose of the Study:

  • To investigate how specific Aβ mutations (Arctic, Italian, Iowa, Flemish) affect aggregate morphology.
  • To compare Aβ aggregation in free solution versus at an anionic surface/liquid interface.
  • To elucidate the role of anionic surfaces in modulating Aβ aggregate polymorphism.

Main Methods:

  • Studied aggregation of wild-type and mutant Aβ peptides.
  • Compared aggregate morphology under free solution conditions.
  • Analyzed aggregation at an anionic mica surface/liquid interface.

Main Results:

  • Mutations altered Aβ aggregation rates in free solution but yielded similar aggregate morphologies.
  • Aggregation on a negatively charged mica surface produced distinct aggregate morphologies for different Aβ mutants.
  • The presence of an anionic surface significantly influenced the structural outcome of Aβ aggregation.

Conclusions:

  • While mutations affect Aβ aggregation kinetics, their impact on morphology is context-dependent.
  • Anionic surfaces play a critical role in dictating the specific polymorphic structures formed by mutant Aβ peptides.
  • These findings offer insights into how surface interactions may contribute to the diverse pathologies observed in Alzheimer's disease.