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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
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...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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 l: Introduction01:29

Alzheimer Disease l: Introduction

Alzheimer disease is a chronic, progressive, and irreversible neurodegenerative disorder and the most common cause of dementia in older adults. It leads to gradual neuronal loss, causing cognitive decline, behavioral changes, and loss of functional independence.Risk Factors and EtiologyThe disease is multifactorial. Age is the strongest risk factor, with prevalence doubling every 5 years after age 65. Genetic factors include mutations in genes such as APP, PSEN1, and PSEN2, which are associated...
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...

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Related Experiment Video

Updated: Jun 9, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Amyloid Fibril Design: Limiting Structural Polymorphism in Alzheimer's Aβ Protofilaments.

Bartłomiej Tywoniuk1,2, Ye Yuan1,2, Sarah McCartan1,2

  • 1School of Physics , University College Dublin , Dublin D04 V1W8 , Ireland.

The Journal of Physical Chemistry. B
|October 19, 2018
PubMed
Summary

Researchers identified minimal mutations to control amyloid fibril structures, crucial for Alzheimer's disease research. This approach stabilizes specific fibril types, aiding drug development and biomarker discovery.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease
06:52

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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

Area of Science:

  • Biophysics
  • Computational Biology
  • Neuroscience

Background:

  • Amyloid peptides form polymorphic fibrils, complicating structural determination and therapeutic development for diseases like Alzheimer's.
  • Controlling amyloid fibril structure is essential for understanding disease mechanisms and designing targeted interventions.

Purpose of the Study:

  • To identify sequence mutations that stabilize specific amyloid fibril structures and reduce polymorphism.
  • To develop a rational strategy for controlling amyloid fibril morphology for therapeutic and diagnostic applications.

Main Methods:

  • Utilized various contact potentials to screen minimal sequence mutations for enhancing specific fibril stabilities.
  • Employed a two-step multiscale approach combining residue and atomistic-level simulations.
  • Validated predictions using atomistic molecular dynamics with explicit water molecules and solid-state NMR data.

Main Results:

  • Identified consensus mutations that bias amyloid-beta (Aβ) fibril packing towards parallel or antiparallel arrangements.
  • Demonstrated that different contact potentials consistently rank mutation compatibility with fibril morphologies.
  • Successfully predicted and validated mutations controlling Aβ9-40 fibril core structures.

Conclusions:

  • Minimal sequence mutations can rationally control amyloid fibril structural polymorphism.
  • This approach offers a powerful tool for guiding experimental studies and designing amyloid-based therapeutics or biomarkers.
  • Provides insights into the molecular basis of amyloid fibril polymorphism.