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

Search research articles

Related Experiment Videos

Amyloid under the atomic force microscope.

Walraj S Gosal¹, Sarah L Myers, Sheena E Radford

¹School of Biochemistry and Microbiology, Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK.

Protein and Peptide Letters

|March 7, 2006

Summary

This summary is machine-generated.

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

Author Correction: High-throughput discovery of fluoroprobes that recognize amyloid fibril polymorphs.

Nature chemistry·2026

Same author

Nanopipettes Enable Native Mass Spectrometry Studies of the Intrinsically Disordered Protein α-Synuclein in Biochemical Buffers.

Analytical chemistry·2026

Same author

Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.

Chemical reviews·2026

Same author

Checking in on proteostasis.

Nature structural & molecular biology·2026

Same author

Amyloid fibril polymorphism: Structural mechanisms of assembly and the links to disease.

Current opinion in structural biology·2026

Same author

In silico peptide self-assembly reveals the importance of N-terminal motifs and the inhibition mechanism of the mutation L38M in α-synuclein fibrillation.

Protein science : a publication of the Protein Society·2026

Same journal

Corrigendum to: Reviewing the Context of Molecular Modeling to Enhance the Application of Machine Learning Technologies for Safer Bioinformatics.

Protein and peptide letters·2026

Same journal

Corrigendum to: A Preliminary Study on the Antibacterial Activity of the Secretion of the Levantine Water Frog, <i>Pelophylax bedriagae</i> (Camerano, 1882) (Anura:Ranidae).

Protein and peptide letters·2026

Same journal

Potent Antioxidant and Antibacterial Activities of ≤3 kDa Hydrolyzed Sarcoplasmic Proteins from IPB-D1 Chicken.

Protein and peptide letters·2026

Same journal

Hybrid 3D Bioprinted Scaffolds for the Delivery of Peptide Therapeutics.

Protein and peptide letters·2026

Same journal

Targeting α-Synuclein: Current Strategies and Emerging Therapies for Synucleinopathies.

Protein and peptide letters·2026

Same journal

Biocompatible Excipients from Microalgae: Advancing Protein and Peptide Therapeutics through Sustainable Formulation Strategies.

Protein and peptide letters·2026

See all related articles

Atomic force microscopy (AFM) images biological samples and measures molecular forces. This review covers AFM

Area of Science:

Biophysics
Materials Science
Nanotechnology

Background:

Protein and peptide self-assembly are crucial in amyloid formation.
Amyloid research is a rapidly developing field.
Atomic force microscopy (AFM) offers nanometre resolution imaging and force measurement capabilities.

Purpose of the Study:

To review the application of AFM in studying protein and peptide self-assembly in amyloid formation.
To outline the technical principles of AFM.
To discuss the advantages and disadvantages of AFM in amyloid research.

Main Methods:

Atomic Force Microscopy (AFM) principles.
Imaging of biological samples at nanometre resolution.
Measurement of inter- and intra-molecular forces in various environments.

Related Experiment Videos

Main Results:

AFM is a versatile tool for visualizing amyloid structures.
AFM can quantify forces involved in protein and peptide self-assembly.
The review highlights AFM's strengths and limitations for amyloid research.

Conclusions:

AFM is a valuable technique for advancing amyloid formation studies.
Understanding AFM's capabilities enhances its application in this field.
Further integration of AFM will likely accelerate discoveries in amyloid research.