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Related Concept Videos

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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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Alzheimer's Disease: Overview01:26

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Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Related Experiment Video

Updated: Sep 20, 2025

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Amyloids on Membrane Interfaces: Implications for Neurodegeneration.

Amaresh Kumar Mahakud1,2, Jafarulla Shaikh1,2, V V Rifa Iqbal1,2

  • 1School of Biological Sciences, National Institute of Science Education and Research, Bhubaneswar, India.

The Journal of Membrane Biology
|June 7, 2022
PubMed
Summary

Amyloid interactions with neuronal membranes are crucial in Alzheimer's and Parkinson's diseases. Understanding these membrane-amyloid dynamics is key to unraveling disease mechanisms and developing therapies.

Keywords:
Amyloid beta (Aβ)Intrinsically disordered proteins (IDP)Neuronal membraneProtein aggregationTauα-Synuclein

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Membrane interfaces are critical for cellular functions.
  • Amyloidogenic proteins in neurodegenerative diseases like Alzheimer's and Parkinson's interact with neuronal membranes.
  • The precise mechanisms governing these membrane-amyloid interactions are not well understood.

Purpose of the Study:

  • To review the multifaceted interactions between amyloids and neuronal membranes.
  • To focus on amyloid-beta (Aβ) peptides and Tau in Alzheimer's disease, and α-synuclein in Parkinson's disease.
  • To consolidate current knowledge on these interactions.

Main Methods:

  • Discussion of genetic studies.
  • Analysis of cell biological findings.
  • Review of biochemical and biophysical studies.

Main Results:

  • Amyloidogenic proteins interact with neuronal membranes in various ways.
  • These interactions influence the onset and progression of neurodegenerative diseases.
  • Current understanding is based on diverse experimental approaches.

Conclusions:

  • Membrane-amyloid interactions are central to neurodegenerative disease pathogenesis.
  • Further research into these interactions is essential for therapeutic development.
  • A comprehensive understanding requires integrating genetic, cellular, biochemical, and biophysical data.