Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Amyloid Fibrils

Amyloid Fibrils

Amyloid Fibrils

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,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

[Intraoperative video fluorescence angiography: a method for predicting the failure of intestinal anastomoses in gunshot wounds to the small intestine].

Khirurgiia·2026

Same author

The Potential of the Peptide Drug Semax and Its Derivative for Correcting Pathological Impairments in the Animal Model of Alzheimer's Disease.

Acta naturae·2026

Same author

PepString Server As a Tool to Search for Short Amino Acid Subsequences: Identification of Potential Amyloid-Beta Targets.

Acta naturae·2025

Same author

The Features of Beta-Amyloid Phosphorylation in Alzheimer's Disease.

Acta naturae·2024

Same author

[Low-Molecular Thiols as a Factor Improving the Sensitivity of Escherichia coli Mutants with Impaired ADP-Heptose Synthesis to Antibiotics].

Molekuliarnaia biologiia·2023

Same author

[Metabolic Stress of Red Blood Cells Induces Hemoglobin Glutathionylation].

Molekuliarnaia biologiia·2023

Search research articles

Related Experiment Video

Updated: Apr 12, 2026

Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease

Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease

Published on: April 19, 2021

[Physico-chemical methods for studing β-amyloid aggregation].

S P Radko¹, S A Khmeleva², E V Suprun²

¹Institute of Biomedical Chemistry, Moscow, Russia; Engelhardt Institute of Molecular Biology, Moscow, Russia.

Biomeditsinskaia Khimiia

|May 16, 2015

Summary

Investigating Alzheimer's disease pathogenesis, this study reviews methods for analyzing beta-amyloid (Aβ) aggregation. Combining techniques offers the most comprehensive understanding of Aβ peptide aggregation in vitro.

Keywords:

Alzheimer's disease aggregation analytical methods b-amyloid

More Related Videos

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

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

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

Related Experiment Videos

Last Updated: Apr 12, 2026

Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease

Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease

Published on: April 19, 2021

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

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

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:

Neurodegenerative disease research
Biochemistry of protein aggregation

Background:

Alzheimer's disease (AD) is a leading neurodegenerative disorder.
The amyloid cascade hypothesis implicates beta-amyloid (Aβ) peptide aggregation in AD pathogenesis.
Understanding Aβ aggregation mechanisms is crucial for AD research.

Purpose of the Study:

To review and compare various in vitro physico-chemical methods for analyzing Aβ aggregation.
To highlight the strengths and limitations of different analytical techniques.
To emphasize the benefits of complementary methods for studying Aβ aggregation.

Main Methods:

Review of established and novel physico-chemical methods.
Analysis includes microscopy, optical, fluorescent, electron paramagnetic resonance, electrochemical, electrophoretic, gel-filtration, and mass spectrometric techniques.
Specific focus on Atomic Force Microscopy (AFM), Fluorescence Correlation Spectroscopy (FCS), and Ion Mobility Mass Spectrometry (IM-MS).

Main Results:

Various methods offer insights into Aβ aggregate size, molecular structure, and morphology.
AFM and FCS allow simultaneous observation of Aβ monomers, oligomers, and larger aggregates.
FCS demonstrates high sensitivity for detecting aggregation at low peptide concentrations.
IM-MS provides data on Aβ oligomer spectrum and structure.

Conclusions:

No single method is sufficient for comprehensive Aβ aggregation analysis.
Combining complementary methods provides the most robust experimental approach.
Advanced techniques like FCS and IM-MS offer unique advantages for studying Aβ aggregation dynamics and structure.