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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated...
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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Actin Filament Depolymerization01:19

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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
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Analysis of &#946;-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
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Static and dynamic disorder in Aβ40 fibrils.

Hui Xiao1, Lan Duo1, James Zhen1

  • 1Department of Neurology, Brain Research Institute, Molecular Biology Institute, University of California, Los Angeles, CA, 90095, USA.

Biochemical and Biophysical Research Communications
|April 23, 2022
PubMed
Summary

Researchers used EPR spectroscopy to analyze amyloid-beta 40 (Aβ40) fibrils, revealing highly ordered structures. This provides insights into Alzheimer's disease mechanisms and potential therapeutic targets.

Keywords:
Alzheimer's diseaseAmyloid fibrilsAβEPRProtein aggregation

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Area of Science:

  • Biophysics
  • Neuroscience
  • Structural Biology

Background:

  • Amyloid-beta (Aβ) fibril deposition is a key feature of Alzheimer's disease.
  • Understanding Aβ fibril structure and dynamics is crucial for developing Alzheimer's therapies.

Purpose of the Study:

  • To investigate the structure and dynamics of Aβ40 fibrils using site-directed spin labeling and EPR spectroscopy.
  • To compare the structural characteristics of Aβ40 and Aβ42 fibrils.

Main Methods:

  • Site-directed spin labeling of Aβ40 peptides.
  • Electron Paramagnetic Resonance (EPR) spectroscopy.
  • Spectral simulations to analyze spin exchange and mobility.

Main Results:

  • Aβ40 fibrils, except for residue D1, are highly ordered.
  • Hydrophobic regions (residues 17-20 and 31-36) exhibit minimal static disorder.
  • Aβ40 fibrils show more ordered packing than Aβ42 fibrils, with an ordered C-terminus.
  • Residues 22 and 23 display the highest dynamic disorder.

Conclusions:

  • Static disorder, not dynamic disorder, primarily influences spin exchange in Aβ40 fibrils.
  • Structural differences, particularly in the C-terminus, may explain why Aβ42 fibrils are more prone to aggregation and defects.
  • Findings offer insights into Alzheimer's pathogenesis and potential therapeutic interventions targeting fibril structure.