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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...
Protein Folding01:22

Protein Folding

Overview
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
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Micelles01:30

Micelles

Micelle formation is an intricate process that hinges on the properties of amphiphilic or amphipathic molecules and the conditions of the system in which they are found. Amphiphilic molecules, which have both hydrophilic (water-attracting) and hydrophobic (water-repelling) parts, play a critical role in this process.In aqueous environments, these molecules arrange themselves such that their hydrophilic heads are turned towards the water phase, while their hydrophobic tails are oriented away...
Protein Organization01:13

Protein Organization

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Related Experiment Video

Updated: May 24, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

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

Published on: March 21, 2025

Peptide-surfactant interactions: consequences for the amyloid-beta structure.

Sandra Rocha1, Joana A Loureiro, Gerald Brezesinski

  • 1LEPAE, Department of Chemical Engineering, Faculty of Engineering, University of Porto, Rua Roberto Frias, Porto, Portugal. sandra.rocha@fe.up.pt

Biochemical and Biophysical Research Communications
|March 13, 2012
PubMed
Summary

Amyloid-beta peptide (Aβ) conformation, crucial for toxic aggregate formation, is modulated by surfactant environments. Ionic micelles induce α-helix structures, while uncharged micelles and high peptide concentrations favor β-sheets.

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A11-positive &#946;-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

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Last Updated: May 24, 2026

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

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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
06:34

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

Area of Science:

  • Biochemistry
  • Materials Science
  • Neuroscience

Background:

  • Amyloid-beta peptide (Aβ) conformation dictates the formation of toxic aggregates implicated in neurodegenerative diseases.
  • Understanding Aβ secondary structure is vital for developing therapeutic strategies.

Purpose of the Study:

  • To characterize the secondary structure of Aβ-(1-40) in various surfactant solutions and at interfaces.
  • To elucidate the influence of environmental factors, specifically surfactants, on Aβ conformation.

Main Methods:

  • Secondary structure analysis of Aβ-(1-40) using spectroscopic techniques.
  • Investigation of Aβ-(1-40) interactions with ionic and uncharged surfactant micelles.
  • Characterization of Aβ-(1-40) adsorption and conformation at ionic monolayers.

Main Results:

  • Aβ-(1-40) adopts β-sheet structures in sub-micellar ionic surfactant solutions and with uncharged micelles.
  • Ionic micelles induce an α-helix structure in Aβ-(1-40).
  • Aβ-(1-40) influences surfactant properties (e.g., critical micelle concentration), indicating hydrophobic interactions.

Conclusions:

  • Surfactant type and micelle charge significantly impact Aβ-(1-40) secondary structure.
  • Electrostatic interactions with fully surrounding charged micelles are key to inducing non-aggregated α-helix structures.
  • Environmental modulation of Aβ conformation offers potential for controlling aggregation.