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

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: May 11, 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

Atomic force microscopy assays for evaluating polyglutamine aggregation in solution and on surfaces.

Kathleen A Burke1, Justin Legleiter

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

Methods in Molecular Biology (Clifton, N.J.)
|May 31, 2013
PubMed
Summary
This summary is machine-generated.

Polyglutamine (polyQ) expansion mutations cause protein misfolding and aggregation in neurodegenerative diseases like Huntington's disease. Atomic force microscopy (AFM) provides detailed analysis of these protein aggregates and their interactions.

More Related Videos

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

Related Experiment Videos

Last Updated: May 11, 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

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

Area of Science:

  • Neuroscience
  • Biochemistry
  • Biophysics

Background:

  • CAG triplet repeat expansions encoding polyglutamine (polyQ) are linked to neurodegenerative diseases.
  • Protein misfolding and aggregation are key pathological features in disorders like Huntington's disease (HD) and spinocerebellar ataxias (SCAs).

Purpose of the Study:

  • To describe detailed protocols for analyzing the aggregation of mutant huntingtin (htt) fragments and synthetic polyQ peptides using atomic force microscopy (AFM).
  • To investigate the formation, morphology, and surface interactions of polyQ aggregates.

Main Methods:

  • Utilizing ex situ AFM to characterize htt aggregate formation and morphology.
  • Employing in situ AFM for real-time tracking of polyQ peptide aggregate formation and fate.
  • Investigating htt interactions with lipid bilayers and their mechanical impact using specialized AFM techniques.
  • Presenting methods for analyzing AFM images of htt aggregates.

Main Results:

  • AFM enables detailed characterization of htt aggregate morphology and formation.
  • In situ AFM allows observation of individual polyQ aggregate dynamics.
  • The interaction of htt with lipid surfaces and its mechanical effects can be quantified.

Conclusions:

  • AFM is a powerful tool for studying polyQ protein aggregation in neurodegenerative diseases.
  • These protocols facilitate the comprehensive analysis of aggregate formation, morphology, and interactions with biological surfaces.