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 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

Single-molecule fluorescence spectroscopy and imaging of heterogeneous amyloid β aggregation.

Methods in enzymology·2026

Same author

Cooperative Native Contact Formation Facilitates Free Energy Barrier Crossing in Protein Folding.

Physical review letters·2026

Same author

Dynamic control of IDP interaction network via diverse binding pathways.

Nature communications·2026

Same author

Single-fibril Förster resonance energy transfer imaging and deep learning reveal concentration dependence of amyloid β 42 aggregation pathways.

PNAS nexus·2025

Same author

Editorial overview.

Current opinion in structural biology·2025

Same author

Three-color single-molecule maximum likelihood analysis of folding and binding of diffusing molecules.

Biophysical journal·2025

Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026

Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026

Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026

Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026

Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026

Same journal

Tuning the physicochemical properties of rationally designed protein-based biomolecular condensates.

Current opinion in structural biology·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 7, 2025

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

Characterizing heterogeneity in amyloid formation processes.

Hoi Sung Chung¹

¹Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892-0520, USA.

Current Opinion in Structural Biology

|November 20, 2024

Summary

This summary is machine-generated.

Understanding protein aggregation, a key factor in diseases, requires characterizing its complex pathways. New methods are improving our understanding of amyloid formation and its intermediates.

More Related Videos

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

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

Published on: April 28, 2022

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

Related Experiment Videos

Last Updated: Jun 7, 2025

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

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

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

Published on: April 28, 2022

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

Area of Science:

Biochemistry and Molecular Biology
Structural Biology
Neuroscience

Background:

Protein aggregation involves numerous pathways from monomers to amyloid fibrils.
Atomic resolution structures of fibril polymorphs are known, but intermediate stages like oligomers are not.
Characterizing aggregation heterogeneity is vital for understanding disease mechanisms and developing therapeutics.

Purpose of the Study:

To review recent advancements in characterizing heterogeneity during amyloid formation.
To highlight the importance of studying intermediate aggregation states.

Main Methods:

Review of recent developments in structure determination techniques.
Focus on methods applicable to heterogeneous protein aggregation processes.
Discussion of solid-state NMR and cryo-electron microscopy (cryoEM) in structural studies.

Main Results:

Advances in techniques like solid-state NMR and cryoEM enable atomic-level structural determination of amyloid fibrils.
Significant gaps remain in understanding the heterogeneous nature of intermediate species, such as oligomers.
The review synthesizes current knowledge on characterizing these complex aggregation pathways.

Conclusions:

Accurate characterization of heterogeneity in protein aggregation is crucial.
Further research into intermediate species is needed for a comprehensive understanding.
Elucidating these processes is key for identifying therapeutic targets for amyloid-related diseases.