Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...
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...

You might also read

Related Articles

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

Sort by
Same author

Discovery of Zilucoplan: A Complement C5 Inhibitor for Treatment of Anti-Acetylcholine Receptor (AChR) Antibody-Positive Generalized Myasthenia Gravis (gMG).

Journal of medicinal chemistry·2025
Same author

AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins.

Protein science : a publication of the Protein Society·2025
Same author

Redox-responsive liposomes aimed at nitroreductase for contents release.

Journal of liposome research·2025
Same author

Monitoring Molecular Interactions with Cell Membranes Using Time-Dependent Second Harmonic Generation Microscopy.

Biochemistry·2025
Same author

Equipping a Wyatt multiangle, multidetector instrument for real-time particle and polymer sizing by simultaneous multiple-angle dynamic and static light scattering.

The Review of scientific instruments·2024
Same author

Solubilization of Paclitaxel with Natural Compound Rubusoside toward Improving Oral Bioavailability in a Rodent Model.

Pharmaceutics·2024
Same journal

Tracking Synthetic Adhesins on Bacterial Surfaces with Immunofluorescence Microscopy.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Post-Selection Methods for Analyzing mRNA Display Selections and Optimization of Hits.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

High-Performance Computing in Tandem Mass Spectrometry (MS/MS) Peptide Identification.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Engineering and Adapting Disulfide-Containing Proteins to Enable Intracellular Functionality.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

AI-Driven Protein Research: From Prediction to Design.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Methods for the In Vitro Selection of Protein and Peptide Libraries Using mRNA Display.

Methods in molecular biology (Clifton, N.J.)·2026
See all related articles

Related Experiment Video

Updated: Jul 3, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Beta-amyloid protein aggregation.

Marcus A Etienne1, Nadia J Edwin, Jed P Aucoin

  • 1Department of Chemistry, Louisiana State University, Baton Rouge, USA.

Methods in Molecular Biology (Clifton, N.J.)
|July 9, 2008
PubMed
Summary
This summary is machine-generated.

This study details a reliable method for producing monomeric beta-amyloid (Abeta) for Alzheimer's disease research. The protocol uses organic solvents and buffer systems, enabling further physical and biological characterization of Abeta aggregation.

More Related Videos

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Related Experiment Videos

Last Updated: Jul 3, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Area of Science:

  • Biochemistry
  • Neuroscience
  • Biophysics

Background:

  • Beta-amyloid (Abeta) peptide aggregation is central to Alzheimer's disease pathogenesis.
  • Understanding Abeta nucleation, oligomerization, and fibril formation is crucial.

Purpose of the Study:

  • To establish a reproducible protocol for generating monomeric Abeta.
  • To characterize Abeta nucleation, aggregation, and fibrillization using various techniques.

Main Methods:

  • Modified Abeta preparation using organic solvents and aqueous phosphate buffers.
  • Physical characterization: scanning force microscopy, circular dichroism, transmission electron microscopy, fluorescence spectroscopy, fluorescence photobleaching recovery, dynamic light scattering.
  • Biological characterization: cell viability assays.

Main Results:

  • A modified method yields monomeric Abeta suitable for kinetic studies.
  • Comprehensive characterization of Abeta nucleation, aggregation intermediates, and fibrils.
  • Assessment of the biological activity of different Abeta species.

Conclusions:

  • The presented protocol reliably produces monomeric Abeta for research.
  • The study provides a framework for investigating Abeta aggregation pathways and their link to Alzheimer's disease.
  • Integrated physical and biological methods enable thorough Abeta characterization.