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

Enantiospecific Magnetoconductance Asymmetry in a Racemic Conglomerate Driven by Surface-Assisted Symmetry Breaking.

Journal of the American Chemical Society·2026

Same author

Close-Shell and Biradical Enantiomers for Probing the Chiral-Induced Spin Selectivity Effect.

The journal of physical chemistry letters·2026

Same author

Dynamic breaking of mirror symmetry in spin-dependent electron transport through chiral media causes enantiomeric excesses.

Science advances·2026

Same author

Temperature-Enhanced Coercive Field by Chiral Molecules.

The journal of physical chemistry letters·2026

Same author

Self-Assembly Behavior of Amino Acids on Au (111) Surfaces: A Molecular Dynamics Study.

Langmuir : the ACS journal of surfaces and colloids·2026

Same author

Formation of S- and Z-twist supramolecular micro-ropes by peptide stereoisomers.

Nature communications·2026

Same journal

A pH-Tolerant Nickel-Vanadium Phosphonate Framework for Stable Aqueous Supercapacitor Cycling.

ACS nano·2026

Same journal

Reconfigurable Photoelectric Coaxial Fiber-Based Memristors for Neuromorphic Computing.

ACS nano·2026

Same journal

Multidimensional Emission Control of CsPbI<sub>3</sub> Quantum Dots Using Plasmonic Quasi-Bound States in the Continuum.

ACS nano·2026

Same journal

Reconfigurable 2D Floating-Gate Field-Effect Transistors with Graphene-Induced Interfacial Polarization for Unified Memory-Logic Integration.

ACS nano·2026

Same journal

Bioinstructive Hybrid Scaffold Integrating Phosphoinositide 3-Kinase-Akt and Complementary Survival Pathways for Kidney Regeneration.

ACS nano·2026

Same journal

Robust Quantum Cutting via Halide-Bearing Ligand Passivation and Gradient Halide Reconstruction for Ultrabroadband Ultraviolet-to-Near-Infrared Photodetection and Imaging.

ACS nano·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Sep 13, 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

Controlling Amyloid Assembly Dynamics Using Spin Interfaces.

Yael Kapon¹, Dror Merhav¹, Gal Finkelstein-Zuta²

¹Institute of Applied Physics, The Hebrew University, Jerusalem 9190401, Israel.

|July 28, 2025

Summary

This summary is machine-generated.

Electron spin interactions influence amyloid fibril formation. Ferromagnetic substrates and monomer chirality control A-β(1-42) self-assembly, offering new therapeutic strategies for neurodegenerative diseases.

Keywords:

Chiral-Induced Spin Selectivity (CISS)amyloids self-assembly spin interactions spin interfaces spin-controlled assembly dynamics

More Related Videos

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Related Experiment Videos

Last Updated: Sep 13, 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

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Area of Science:

Biophysics
Materials Science
Neuroscience

Background:

Protein aggregation into amyloid fibrils is implicated in diseases like Alzheimer's.
The influence of electron spin interactions on amyloid formation is not well understood.

Purpose of the Study:

To investigate the role of electron spin interactions in amyloid fibril formation of A-β(1-42) polypeptide.
To explore the impact of ferromagnetic substrates on fibril nucleation and self-assembly.

Main Methods:

Studied amyloid formation of A-β(1-42) and its recognition motifs on ferromagnetic substrates.
Utilized electron and fluorescence microscopy to observe fibril dynamics.
Employed ATR-FTIR to detect structural variations in fibrils.

Main Results:

Fibril formation showed strong dependence on substrate magnetization orientation.
One orientation yielded twice as many and 20-fold longer fibrils compared to the opposite.
These effects were modulated by monomer chirality and influenced fibril structure.

Conclusions:

Transient spin polarization, potentially via the Chiral-Induced Spin Selectivity (CISS) effect, is critical for amyloid assembly.
Spin-based influences on biomolecular aggregation are fundamental and scale-independent.
Potential therapeutic applications include spin-polarized nanoparticles for neurodegenerative diseases and spin-selective interfaces for dialysis systems.