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

Atomic Force Microscopy01:08

Atomic Force Microscopy

Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
The AFM Probe
The probe is regarded as the heart of any AFM setup and comprises the...

You might also read

Related Articles

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

Sort by
Same author

Proteomic Impact of Peripheral Expression of Mutant Huntingtin in <i>C. elegans</i>.

Journal of proteome research·2026
Same author

STIP1/HOP promotes the formation of cytotoxic α-synuclein oligomers.

Molecular neurodegeneration advances·2026
Same author

Toward Metabolomics Analyses With Combined Capillary Vibrating Sharp-Edge Spray Ionization and Atmospheric Pressure Chemical Ionization.

Rapid communications in mass spectrometry : RCM·2026
Same author

Exogenous Huntingtin-Exon1 Aggregates Exhibit Distinct Levels of Toxicity to <i>Caenorhabditis elegans</i>.

ACS chemical neuroscience·2025
Same author

Membranes as targets and modifiers of mutant huntingtin aggregation.

Trends in biochemical sciences·2025
Same author

Amyloidogenic SARS-CoV-2 Spike Protein-Derived Peptides Form Oligomers and Selectively Damage Lipid Membranes.

Biochemistry·2025

Related Experiment Video

Updated: Jun 7, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Assessing Aβ aggregation state by atomic force microscopy.

Justin Legleiter1

  • 1The C. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, WV, USA.

Methods in Molecular Biology (Clifton, N.J.)
|October 23, 2010
PubMed
Summary
This summary is machine-generated.

Atomic force microscopy (AFM) is ideal for studying conformational diseases like Alzheimer's by visualizing protein aggregates. AFM tracks the aggregation of amyloid-beta peptides in real-time, offering insights into disease mechanisms.

More Related Videos

Analysis of &#946;-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Related Experiment Videos

Last Updated: Jun 7, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Analysis of &#946;-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Area of Science:

  • Biophysics
  • Neuroscience
  • Materials Science

Background:

  • Conformational diseases involve protein misfolding and aggregation.
  • Alzheimer's disease is a neurodegenerative conformational disease linked to amyloid-beta (Aβ) peptide aggregation.
  • Characterizing protein aggregates is crucial for understanding disease pathogenesis.

Purpose of the Study:

  • To describe the application of atomic force microscopy (AFM) in characterizing protein aggregation.
  • To highlight AFM's capability in studying the amyloid-beta (Aβ) peptide aggregation relevant to Alzheimer's disease (AD).

Main Methods:

  • Utilizing atomic force microscopy (AFM) for high-resolution imaging of protein aggregates.
  • Employing AFM in both ex situ (air) and in situ (solution) modes to study aggregation dynamics.
  • Tracking the morphological changes and evolution of individual aggregates over time.

Main Results:

  • AFM effectively distinguishes various aggregate forms, from small oligomers to mature amyloid fibrils.
  • In situ AFM allows dynamic monitoring of the real-time aggregation process.
  • Characterization of Aβ peptide aggregation using AFM provides structural insights.

Conclusions:

  • AFM is a powerful tool for analyzing the nanoscale structures of protein aggregates in conformational diseases.
  • AFM's dynamic imaging capabilities in solution are vital for understanding aggregation pathways.
  • This approach aids in elucidating the role of Aβ aggregation in Alzheimer's disease.