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, normally used to...

You might also read

Related Articles

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

Sort by

Same author

Paediatric Cardiac Tumours: A National Population Study.

Pediatric cardiology·2025

Same author

POLYPHARMACY AND CANCER: А NEW VISION FOR SKIN CANCER PATHOGENESIS-PHOTOTOXICITY AND PHOTOCARCINOGENICITY DUE TO NITROSAMINE CONTAMINATION DURING TELMISARTAN/ TAMSULOSIN INTAKE.

Georgian medical news·2025

Same author

Efficacy of neuromuscular exercises to promote movement quality and reduce musculoskeletal injury during initial military training in Royal Navy recruits.

BMJ military health·2024

Same author

Unrecognized volatile and semi-volatile organic compounds from brake wear.

Environmental science. Processes & impacts·2024

Same author

Symptom burden, management and treatment goals of people with MS spasticity: Results from SEEN-MSS, a large-scale, self-reported survey.

Multiple sclerosis and related disorders·2022

Same author

Investigating dysphagia in adults: symptoms and tests.

BMJ (Clinical research ed.)·2022

Search research articles

Related Experiment Video

Updated: Jul 20, 2026

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 13, 2010

De novo amyloid proteins from designed combinatorial libraries.

M W West¹, W Wang, J Patterson

¹Department of Chemistry, Princeton University, Princeton, NJ 08544-1009, USA.

Proceedings of the National Academy of Sciences of the United States of America

|September 29, 1999

Summary

Scientists created novel amyloid-like fibrils using designed protein sequences. Alternating polar and nonpolar residues drive this self-assembly, offering insights into neurodegenerative disease mechanisms.

More Related Videos

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Related Experiment Videos

Last Updated: Jul 20, 2026

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 13, 2010

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Area of Science:

Biochemistry
Molecular Biology
Neuroscience

Background:

Amyloid deposits are hallmarks of neurodegenerative diseases like Alzheimer's disease and prion diseases.
Amyloid fibrils share structural similarities despite differing protein sequences across diseases.

Purpose of the Study:

To investigate the relationship between amino acid sequence and amyloid formation propensity.
To design and characterize de novo protein sequences that self-assemble into amyloid-like structures.

Main Methods:

Created a combinatorial library of protein sequences with alternating polar and nonpolar residues.
Utilized electron microscopy to visualize self-assembled oligomers as fibrils.
Assessed fibril structure using Congo red binding and secondary structure analysis (beta-sheet).

Main Results:

De novo designed sequences self-assembled into amyloid-like fibrils.
These fibrils exhibited structural characteristics of natural amyloid, including beta-sheet content and Congo red binding.
Fibril assembly and disassembly were found to be reversible.

Conclusions:

Alternating patterns of polar and nonpolar residues can direct protein sequences to form amyloid-like fibrils.
This reversible model system facilitates studies on fibril assembly mechanisms.
The findings support the development of molecular therapies targeting amyloid formation.