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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
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Protein Organization01:13

Protein Organization

Overview

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Related Experiment Video

Updated: Jun 27, 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

Amyloid beta conformation in aqueous environment.

K Takano1

  • 1Department of Material and Life Science, Osaka University, Suita, Japan. ktakano@mls.eng.osaka-u.ac.jp

Current Alzheimer Research
|December 17, 2008
PubMed
Summary
This summary is machine-generated.

Amyloid beta (Abeta) fibrils are linked to Alzheimer's disease. New methods reveal Abeta peptide structures in water, offering insights into neurotoxicity mechanisms.

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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

Related Experiment Videos

Last Updated: Jun 27, 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

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Amyloid beta (Abeta) peptides aggregate into fibrils, a hallmark of Alzheimer's disease.
  • The atomic-level structure of Abeta in aqueous environments remains challenging to determine due to aggregation.
  • Soluble Abeta forms are reported to possess intrinsic neurotoxicity.

Purpose of the Study:

  • To review current knowledge on Abeta conformation in aqueous environments.
  • To explore structural insights into Abeta's aggregation and neurotoxicity.

Main Methods:

  • Solid-state NMR studies reveal parallel beta-sheet structures in Abeta fibrils.
  • A novel fusion technique with hyperthermophile proteins allows crystal structure determination of Abeta fragments in aqueous solution without organic solvents or detergents.

Main Results:

  • Abeta28-42 fragment forms a beta-conformation in aqueous solution.
  • The fusion technique provides atomic-resolution structural information for amyloidogenic peptides in aqueous environments.

Conclusions:

  • Understanding Abeta conformation in aqueous environments is crucial for Alzheimer's disease research.
  • The reviewed structural data provides viewpoints on Abeta's aggregation and potential neurotoxicity.