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

From Disordered to Ordered: Nanoscale Spectroscopy Reveals Structural Evolution of Amyloid Beta 40 Fibrils.

Chemphyschem : a European journal of chemical physics and physical chemistry·2026

Same author

Lipid mediated formation of antiparallel aggregates in cerebral amyloid angiopathy.

Acta neuropathologica·2025

Same author

Quantification of Protein Secondary Structures from Discrete Frequency Infrared Images Using Machine Learning.

Applied spectroscopy·2025

Same author

Investigating Benzoic Acid Derivatives as Potential Atomic Layer Deposition Inhibitors Using Nanoscale Infrared Spectroscopy.

Nanomaterials (Basel, Switzerland)·2025

Same author

Heterotypic Seeding Generates Mixed Amyloid Polymorphs.

Small science·2025

Same author

Heterotypic Interactions of Amyloid β and the Islet Amyloid Polypeptide Produce Mixed Aggregates with Non-Native Fibril Structure.

The journal of physical chemistry letters·2024

Same journal

Whole-Embryo 3D Quantification Reveals Conserved Topological Design and Scaling of Germ Layers in Xenopus.

bioRxiv : the preprint server for biology·2026

Same journal

scRNA-seq and genomics analyses reveal key mechanisms of inverted papilloma-associated sinonasal squamous cell carcinoma malignant transformation.

bioRxiv : the preprint server for biology·2026

Same journal

M1C IS NECESSARY FOR DARAXONRASIB RESISTANCE OF NSCLC KRAS(G12C) MUTANT CELLS.

bioRxiv : the preprint server for biology·2026

Same journal

A human-specific genetic modifier reconfigures large-scale cortical network dynamics underlying behavioral performance.

bioRxiv : the preprint server for biology·2026

Same journal

<i>Staphylococcus aureus</i> uses a eukaryotic-like uridyltransferase to make UDP-GlcNAc for cell wall synthesis.

bioRxiv : the preprint server for biology·2026

Same journal

Dynamic redistribution of eIF4F controls cap-dependent translation initiation.

bioRxiv : the preprint server for biology·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 29, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Heterotypic Seeding Generates Mixed Amyloid Polymorphs.

S Banerjee¹, D Baghel¹, H O Edmonds¹

¹Department of Chemistry and Biochemistry, The University of Alabama, 1007E Shelby Hall, Tuscaloosa, Alabama 35487, United States.

Biorxiv : the Preprint Server for Biology

|April 1, 2024

Summary

This summary is machine-generated.

Amyloid beta (Aβ) can form complex mixed structures with other proteins, not just its own kind. This finding is crucial for understanding Alzheimer's disease (AD) and developing new treatments.

Keywords:

AFM-IR Alzheimer’s disease amyloid beta infrared spectroscopy nanoscale spectroscopy protein aggregation

More Related Videos

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits

Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits

Published on: March 16, 2016

Related Experiment Videos

Last Updated: Jun 29, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits

Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits

Published on: March 16, 2016

Area of Science:

Biochemistry
Neuroscience
Molecular Biology

Background:

Amyloid beta (Aβ) fibril formation is central to Alzheimer's disease (AD) pathogenesis.
The influence of non-Aβ seeds on Aβ aggregate structure remains poorly understood.
Understanding Aβ aggregation complexity is vital for AD therapeutic development.

Approach:

Utilized nanoscale infrared spectroscopy to analyze individual Aβ aggregates.
Investigated Aβ42 aggregation with antiparallel Aβ (16-22) and E22Q Aβ (1-40) Dutch mutant seeds.
Examined heterotypic aggregation of Aβ with alpha synuclein and brain protein lysates.

Key Points:

Aβ forms heterotypic or mixed polymorphs deviating from the canonical parallel cross-β structure when seeded with structurally different Aβ variants.
Heterotypic aggregate formation extends beyond Aβ isomers, including interactions with alpha synuclein and complex biological mixtures.
These findings reveal intricate Aβ aggregation pathways beyond simple self-assembly.

Conclusions:

The structural diversity of amyloid aggregates is influenced by non-native seeds.
Aβ aggregation is a complex process involving interactions with various brain components.
Further research into Aβ interactions is essential for advancing Alzheimer's disease therapies.