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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,...

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Related Experiment Video

Updated: Oct 16, 2025

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

Plasmonic Amyloid Tactoids.

Ye Yuan¹, Hamed Almohammadi¹, Julie Probst²

¹Department of Health Sciences and Technology, ETH Zürich, Zürich, 8092, Switzerland.

Advanced Materials (Deerfield Beach, Fla.)

|October 18, 2021

Summary

This summary is machine-generated.

Amyloid fibrils, despite disease links, can form functional photonic materials. Ordered fibrils align nanoparticles, enhancing fluorescence and enabling selective optical effects for new material applications.

Keywords:

amyloid fibrils fluorescence gold nanorods liquid crystals plasmonics self-assembly

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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

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

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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

Area of Science:

Biomaterials Science
Nanotechnology
Photonics

Background:

Amyloids, known for neurodegenerative disease links, possess inherent photonic properties.
Natural and synthetic amyloids can be utilized as building blocks for advanced functional materials.

Purpose of the Study:

To explore the potential of amyloid fibrils in creating functional hybrid materials.
To investigate the coupling of amyloid photonic properties with plasmonic nanoparticles.

Main Methods:

Fabrication of orientationally ordered amyloid fibril liquid crystalline phases.
Codispersion of rod-shaped plasmonic nanoparticles with amyloid fibrils.
Characterization of optical properties, including polarization-dependent fluorescence and plasmonic extinction.
Numerical simulations of near-field plasmonic enhancement.

Main Results:

Orientationally ordered amyloid fibrils exhibit polarization-dependent fluorescence.
Amyloid fibrils mechanically align codispersed plasmonic nanoparticles.
Hybrid materials show selective activation of plasmonic extinctions and enhanced fluorescence.
Experimental findings are supported by near-field plasmonic enhancement simulations.

Conclusions:

Amyloid fibrils can be integrated with plasmonic nanoparticles to create functional hybrid materials.
The study demonstrates a method to harness intrinsic photonic and mechanical properties of amyloids.
Enhanced luminescence of amyloid-nanoparticle hybrids may improve amyloid deposit detection.