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Related Concept Videos

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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. 
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Structural Interconversion in Alzheimer's Amyloid-β(16-35) Peptide in an Aqueous Solution.

Nelson A Alves1, Rafael B Frigori2

  • 1Departamento de Fı́sica, FFCLRP, Universidade de São Paulo , Avenida Bandeirantes, 3900, Ribeirão Preto 14040-901, SP, Brazil.

The Journal of Physical Chemistry. B
|January 21, 2018
PubMed
Summary

The amyloid-beta (Aβ) peptide fragment (16-35) directly converts from a disordered coil to a β-sheet structure. This folding pathway lacks helix intermediates and energy barriers, revealing intrinsic disorder in Aβ aggregation.

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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
  • Molecular Biology
  • Computational Chemistry

Background:

  • Amyloid-beta (Aβ) peptides are implicated in Alzheimer's disease.
  • Understanding Aβ peptide structure and folding is crucial for therapeutic development.
  • The Aβ(16-35) fragment serves as a model for studying aggregation, excluding terminal effects.

Purpose of the Study:

  • To investigate the structural properties and folding pathway of the Aβ(16-35) fragment.
  • To elucidate the mechanism of Aβ peptide aggregation.
  • To determine if the Aβ(16-35) fragment exhibits intrinsic disorder.

Main Methods:

  • Replica-exchange molecular dynamics simulations were employed.
  • All-atom and explicit aqueous solvation models were used to minimize structural bias.
  • Principal component analysis was utilized to analyze conformational dynamics.

Main Results:

  • The primary folding pathway involves direct conversion of coil to β-sheet structure.
  • No long helical intermediates were observed in the folding process.
  • The Aβ(16-35) fragment was found to be intrinsically disordered, similar to the full Aβ peptide.
  • The folding mechanism lacks significant free-energy barriers and thermal capacity peaks.

Conclusions:

  • The Aβ(16-35) fragment adopts a β-sheet structure through a direct coil-to-sheet transition.
  • The folding pathway is barrierless and suggests intrinsic disorder.
  • These findings provide insights into the early stages of amyloid-beta aggregation relevant to neurodegenerative diseases.